NCBI Conserved Domain Search

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 258.36 E-value: 4.03e-81

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549    66 LFKGEYLMVNRsIDNNKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGdENSHYINASYVNSWLRDKAYVVTQAvr 143
Cdd:smart00194   1 GLEEEFEKLDR-LKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQG-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   144 tkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPE 217
Cdd:smart00194  77 --PLpstVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   218 siETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFF 296
Cdd:smart00194 155 --ETRTVTHYHYTNWPDHGVPeSPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIF 230

                          250       260
                   ....*....|....*....|....*....
gi 212645549   297 EYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:smart00194 231 EIVKELRSQRPGMVQTEEQYIFLYRAILE 259

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 226.35 E-value: 2.84e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   92 MDRNPYPDTLPYDYNRVILPriDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 168
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQG----PLPntvEDFWRMVWEEKVTIIVMLTE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  169 VFDFMRVMCLQYWPLTKFQ---FREIEVETTEVKTY-SHFVIRTFKLTRTTPEsiETRIVKHFHFTEW-ELDSFPYISAF 243
Cdd:pfam00102  76 LEEKGREKCAQYWPEEEGEsleYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSE--ETRTVKHFHYTGWpDHGVPESPNSL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  244 IELRRRVRQfMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:pfam00102 154 LDLLRKVRK-SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                  ..
gi 212645549  324 SE 325
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: 221.01 E-value: 1.03e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL---TKFQFREIEVE 194
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQG----PLPntvEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEeggKPLEYGDITVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 195 TTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQFMEKNpvEAPMVVHCSNGAGR 273
Cdd:cd00047   77 LVSEEELSDYTIRTLELSPKGCS--ESREVTHLHYTGWPDHGVPsSPEDLLALVRRVRKEARKP--NGPIVVHCSAGVGR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 212645549 274 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd00047  153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 205.97 E-value: 2.93e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   377 DCAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 456
Cdd:smart00194  18 SCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDY--INASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   457 TVVNLSNQGS------QRHYPSFIHnkGKANYGPFIVEIMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVR 530
Cdd:smart00194  96 VIVMLTELVEkgrekcAQYWPDEEG--EPLTYGDITVTLKSVEKVDDYTIRTLEVTNTG----------------CSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   531 ICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFH 610
Cdd:smart00194 158 TVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQS-----TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 212645549   611 AVKMMRINRPQLIDMKDEYKYLYDVMLH 638
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: 198.77 E-value: 6.79e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14553    6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQG----PLPetfGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIE 245
Cdd:cd14553   82 ERSRVKCDQYWPTRGTEtYGLIQVtllDTVELATYT---VRTFALHKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 246 LRRRVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 324
Cdd:cd14553  157 FLRRVKAC---NPPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233


                 ....*
gi 212645549 325 EAVMC 329
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: 181.79 E-value: 3.00e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  62 KKRILFKgEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQA 141
Cdd:cd14543    1 QKRGIYE-EYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 142 VRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTtpES 218
Cdd:cd14543   80 PLPKTYS-DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgssLRYGDLTVTNLSVENKEHYKKTTLEIHNT--ET 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 219 IETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFME-----------KNPVEAPMVVHCSNGAGRSGAFLALDANLEL 286
Cdd:cd14543  157 DESRQVTHFQFTSWPDFGVPSSAAaLLDFLGEVRQQQAlavkamgdrwkGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQ 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 212645549 287 MKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
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: 174.46 E-value: 3.37e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  97 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 176
Cdd:cd14548    2 YTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKD-DFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 177 CLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQF 253
Cdd:cd14548   81 CDHYWPFDQDPvyYGDITVTMLSESVLPDWTIREFKLERGD----EVRSVRQFHFTAWPDHGVPEAPDsLLRFVRLVRDY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645549 254 MEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
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: 173.86 E-value: 9.24e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14554    9 KNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQG----PLAettEDFWRMLWEHNSTIIVMLTKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRR 248
Cdd:cd14554   85 EMGREKCHQYWPAeRSARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSGeGFIDFIG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645549 249 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
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: 6.35e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETL-SDFWRMVWEQRTATIVMMTRLEEKS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTKFQ-FREIEV---ETTEVKTYShfvIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 248
Cdd:cd14626  123 RVKCDQYWPIRGTEtYGMIQVtllDTVELATYS---VRTFALYKNG--SSEKREVRQFQFMAWPDHGVPeYPTPILAFLR 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 249 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14626  198 RVKAC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274


                 ..
gi 212645549 328 MC 329
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: 1.26e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  93 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 169
Cdd:cd14630    5 NKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQG----PMQEtvkDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 170 FDFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFP-YISAFIELRR 248
Cdd:cd14630   81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI--REIRQFHFTSWPDHGVPcYATGLLGFVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 249 RVRqFMekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14630  159 QVK-FL--NPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEAC 235


                 ..
gi 212645549 328 MC 329
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: 161.68 E-value: 9.73e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQRHYPSFIHNKGK-ANYGPFIVEIMNY 492
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlveKGREKCERYWPEEGGKpLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 493 HQYPAMTshmvkvmKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTtglIDVIKMARSWRKRAPDRpe 572
Cdd:cd00047   81 EELSDYT-------IRTLELSPKG---------CSESREVTHLHYTGWP-DHGVPSSP---EDLLALVRRVRKEARKP-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645549 573 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 634
Cdd:cd00047  139 NGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 160.49 E-value: 6.70e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  386 NRGKNRDVMVVPPDHARPYLQtlhGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 463
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  464 ----QGSQRHYPSfiHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMIsdimatgaQNQQIDAEVRiccVIQVRM 539
Cdd:pfam00102  78 ekgrEKCAQYWPE--EEGESLEYGDFTVTLKKEKEDEK------DYTVRTLEV--------SNGGSEETRT---VKHFHY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  540 --WPiENKVPLSTTGLIDVIKMARSWRkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 617
Cdd:pfam00102 139 tgWP-DHGVPESPNSLLDLLRKVRKSS----LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRS 213

                         250       260
                  ....*....|....*....|
gi 212645549  618 NRPQLIDMKDEYKYLYDVML 637
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: 7.93e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 107 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL 183
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQG----PVHEtvyDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 184 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRqfMEKNPVEAP 262
Cdd:cd14631   77 DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYN--EIREVKQFHFTGWPDHGVPYhATGLLSFIRRVK--LSNPPSAGP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 263 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 328
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: 160.11 E-value: 8.14e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  97 YPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVM 176
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVN-DFWRMVWEQKSATIVMLTNLKERKEEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 177 CLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIE-TRIVKHFHFTEWELDSFPYISafIELRRRVRQFM 254
Cdd:cd14620   80 CYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKaPRLVTQLHFTSWPDFGVPFTP--IGMLKFLKKVK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645549 255 EKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 161.80 E-value: 8.46e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14625   50 KNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETF-GDFWRMVWEQRSATVVMMTKLEEKS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTKFQ-FREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRRRVR 251
Cdd:cd14625  129 RIKCDQYWPSRGTEtYGMIQVTLLDTIELATFCVRTFSLHKNG--SSEKREVRQFQFTAWPDHGVPeYPTPFLAFLRRVK 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645549 252 QFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 329
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: 1.57e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14633   43 KNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQG----PMQEtiyDFWRMVWHENTASIIMVTNLV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISAfiELRRRV 250
Cdd:cd14633  119 EVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVH--EIREIRQFHFTGWPDHGVPYHAT--GLLGFV 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645549 251 RQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 328
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: 2.09e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVfDFMRVMCLQYWPL-TKFQFREIEVETT 196
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQH----PLPntvTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDeGSGTYGPIQVEFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 197 EVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGRS 274
Cdd:cd14556   76 STTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRdrDTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 212645549 275 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14556  155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

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

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 159.51 E-value: 7.35e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETF-GDFWRMIWEQRSATVVMMTKLEERS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPL----TKFQFREIEVETTEVKTYshfVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP-YISAFIELRR 248
Cdd:cd14624  129 RVKCDQYWPSrgteTYGLIQVTLLDTVELATY---CVRTFALYKNG--SSEKREVRQFQFTAWPDHGVPeHPTPFLAFLR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 249 RVRQFmekNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14624  204 RVKTC---NPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280


                 ..
gi 212645549 328 MC 329
Cdd:cd14624  281 TC 282

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350480 [Multi-domain] Cd Length: 205 Bit Score: 156.75 E-value: 7.60e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTEVKT 200
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQE-MVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 201 YSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPY----ISAFIelrRRVRQfmeKNPVEA-PMVVHCSNGAGRSG 275
Cdd:cd14632   80 LAEYSVRTFALERRGYSARHE--VKQFHFTSWPEHGVPYhatgLLAFI---RRVKA---STPPDAgPVVVHCSAGAGRTG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645549 276 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVMC 329
Cdd:cd14632  152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 156.97 E-value: 1.11e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 174
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVG-DFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 175 VMCLQYWPL--TKFQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVR 251
Cdd:cd14619   80 VKCEHYWPLdyTPCTYGHLRVTVVSEEVMENWTVREFLLKQV--EEQKTLSVRHFHFTAWPDHGVPSsTDTLLAFRRLLR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 252 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14619  158 QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227

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: 155.07 E-value: 2.77e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 197
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQG----PMQEtvyDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 198 VKTYSHFVIRTFKLTRTTPESIetRIVKHFHFTEWELDSFPYISAfiELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 276
Cdd:cd14555   77 TEPLAEYVVRTFALERRGYHEI--REVRQFHFTGWPDHGVPYHAT--GLLGFIRRVKASNPPSAgPIVVHCSAGAGRTGC 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 328
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: 1.48e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETT 196
Cdd:cd14549    1 YINANYVDGYNKARAYIATQG----PLPStfdDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 197 EVKTYSHFVIRTF-----KLTRTTPESIEtRIVKHFHFTEWE-----LDSFPYISaFielrrrVRQFMEKNPVEA-PMVV 265
Cdd:cd14549   77 STEVLATYTVRTFslknlKLKKVKGRSSE-RVVYQYHYTQWPdhgvpDYTLPVLS-F------VRKSSAANPPGAgPIVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 266 HCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14549  149 HCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 153.66 E-value: 1.96e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 101 LPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQY 180
Cdd:cd14623    6 IPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIE-DFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 181 WPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNP 258
Cdd:cd14623   85 WPSDgSVSYGDITIELKKEEECESYTVRDLLVTNTREN--KSRQIRQFHFHGWPEVGIPSDgKGMINIIAAV-QKQQQQS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 259 VEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14623  162 GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

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: 2.62e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 174
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIE-DFWRLVWEQQVCNIIMLTVGMENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 175 VMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFP----YISAFIELrr 248
Cdd:cd14618   80 VLCDHYWPseSTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLR--KERRVKHLHYTAWPDHGIPestsSLMAFREL-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645549 249 rVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14618  156 -VREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 152.16 E-value: 3.27e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTE 197
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQG----PLPdtiADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 198 VKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPyiSAFIELRRRVRQ----FMEKNPVEAPMVVHCSNG 270
Cdd:cd14558   77 TEKSPTYTVRVFEITHL--KRKDSRTVYQYQYHKWkgeELPEKP--KDLVDMIKSIKQklpyKNSKHGRSVPIVVHCSDG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212645549 271 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
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: 1.36e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 199
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVE-DFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 278
Cdd:cd14552   80 DYEDYTLRDFLVTKGKGGS--TRTVRQFHFHGWPEVGIPDnGKGMIDLIAAV-QKQQQQSGNHPITVHCSAGAGRTGTFC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645549 279 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14552  157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

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

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 151.42 E-value: 6.75e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14629   56 KNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE-DFWRMLWEHNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 251
Cdd:cd14629  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTIRQFQFTDWPEQGVPKTgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 252 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 1.85e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMR 174
Cdd:cd14615    1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVK-DFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 175 VMCLQYWPLT-KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQ 252
Cdd:cd14615   79 TKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--TNESRTVRHFHFTSWPDHGVPETTdLLINFRHLVRE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 253 FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFI 319
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: 149.88 E-value: 1.92e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14627   56 KNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWENNSTIVVMLTKLREMG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 251
Cdd:cd14627  135 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 252 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14627  213 KTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286

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

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 149.88 E-value: 2.39e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKpMNAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14628   55 KNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAE-TTEDFWRMLWEHNSTIVVMLTKLREMG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYI-SAFIELRRRVR 251
Cdd:cd14628  134 REKCHQYWPAERsARYQYFVVDPMAEYNMPQYILREFKVTDA--RDGQSRTVRQFQFTDWPEQGVPKSgEGFIDFIGQVH 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 252 QFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14628  212 KTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285

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: 5.40e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILPRIDGDENSHYINASYV--NSWLRDkaYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKV 169
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIpgNNFRRE--YIATQG----PLPGtkdDFWKMVWEQNVHNIVMVTQC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 170 FDFMRVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTrtTPESIET-RIVKHFHFTEWELDSFPYIS-AFIE 245
Cdd:cd14617   75 VEKGRVKCDHYWPADQdsLYYGDLIVQMLSESVLPEWTIREFKIC--SEEQLDApRLVRHFHYTVWPDHGVPETTqSLIQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 246 LRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14617  153 FVRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

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: 2.08e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDenSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSG-HFWQMVWEQNSKAVIMLNKLMEKG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPL-----TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELR 247
Cdd:cd14545   78 QIKCAQYWPQgegnaMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQ--ETREVLHFHYTTWPDFGVPESpAAFLNFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 248 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPH---LIDSVEQYMFIY 320
Cdd:cd14545  156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEK-GNPSSVDVKKVLLEMRKYrmgLIQTPDQLRFSY 230

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

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 140.53 E-value: 4.60e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 199
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVE-DFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEgSVTHGEITIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYI-SAFIELRRRVrQFMEKNPVEAPMVVHCSNGAGRSGAFL 278
Cdd:cd14622   81 LLETISIRDFLVTYNQEK--QTRLVRQFHFHGWPEIGIPAEgKGMIDLIAAV-QKQQQQTGNHPIVVHCSAGAGRTGTFI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 212645549 279 ALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14622  158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

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

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 142.10 E-value: 9.24e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSH--YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 171
Cdd:cd17667   30 KNRYINILAYDHSRVKLRPLPGKDSKHsdYINANYVDGYNKAKAYIATQG-PLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 172 FMRVMCLQYWPL-TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESIET---------RIVKHFHFTEWELDSFP-YI 240
Cdd:cd17667  109 KGRRKCDQYWPTeNSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnpkgrqneRTVIQYHYTQWPDMGVPeYA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 241 SAFIELRRRVRQfmEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
Cdd:cd17667  189 LPVLTFVRRSSA--ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 266


                 ....*...
gi 212645549 321 EVLSEAVM 328
Cdd:cd17667  267 DALLEAIL 274

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.

Pssm-ID: 350395 [Multi-domain] Cd Length: 224 Bit Score: 139.07 E-value: 2.56e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSW-LRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQG----PLPntvADFWRMVWQEKTPIIVMITNLT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DfMRVMCLQYWP-LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYIS-AFIELRR 248
Cdd:cd14547   77 E-AKEKCAQYWPeEENETYGDFEVTVQSVKETDGYTVRKLTLKYGG----EKRYLKHYWYTSWPDHKTPEAAqPLLSLVQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645549 249 RVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
Cdd:cd14547  152 EVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

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: 3.58e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14614   15 KNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRN-DFWKMVLQQKSQIIVMLTQCNEKR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPLTK--FQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA---FIELRR 248
Cdd:cd14614   94 RVKCDHYWPFTEepVAYGDITVEMLSEEEQPDWAIREFRVSYAD----EVQDVMHFNYTAWPDHGVPTANAaesILQFVQ 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645549 249 RVRQFMEKNPveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14614  170 MVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

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: 135.45 E-value: 3.72e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVN-SWLRDKAYVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFR--EIEVE 194
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQG----PLPAtigDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEygDLTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 195 TTEVKTYSH--FVIRTFKLTRTTPESietRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVEAPMVVHCSNGA 271
Cdd:cd18533   77 LVSEEENDDggFIVREFELSKEDGKV---KKVYHIQYKSWpDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 272 GRSGAFLALDANLELMKKTGQLDFFEY------AKTlVNS----RPHLIDSVEQYMFIYE 321
Cdd:cd18533  154 GRTGTFIALDSLLDELKRGLSDSQDLEdsedpvYEI-VNQlrkqRMSMVQTLRQYIFLYD 212

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 137.85 E-value: 3.79e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  93 DRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDF 172
Cdd:cd14621   54 EKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVN-DFWRMIWEQNTATIVMVTNLKER 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 173 MRVMCLQYWPLTK-FQFREIEVETTEVKTYSHFVIRTF------KLTRTTPEsietRIVKHFHFTEWELDSFPYISafIE 245
Cdd:cd14621  133 KECKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQ----RLITQFHFTSWPDFGVPFTP--IG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 246 LRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 324
Cdd:cd14621  207 MLKFLKKVKNCNPQYAgAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                 .
gi 212645549 325 E 325
Cdd:cd14621  287 E 287

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 135.15 E-value: 2.72e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  93 DRNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKV 169
Cdd:cd14608   27 NRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQG----PLPntcGHFWEMVWEQKSRGVVMLNRV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 170 FDFMRVMCLQYWPltKFQFREIEVETTEVK-------TYSHFVIRTFKLTRTTPEsiETRIVKHFHFTEWELDSFPYISA 242
Cdd:cd14608   99 MEKGSLKCAQYWP--QKEEKEMIFEDTNLKltlisedIKSYYTVRQLELENLTTQ--ETREILHFHYTTWPDFGVPESPA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 243 -FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPH---LIDSVEQYMF 318
Cdd:cd14608  175 sFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFrmgLIQTADQLRF 254


                 ..
gi 212645549 319 IY 320
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: 5.92e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLsNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhq 494
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDqsCPQYWPDEGSGTYGPIQVEFVS--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 ypamTSHMVKVMKRTFMISDIMATgaqnqqiDAEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpetK 574
Cdd:cd14556   77 ----TTIDEDVISRIFRLQNTTRP-------QEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGE----G 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 575 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 634
Cdd:cd14556  142 PIVVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 131.19 E-value: 7.77e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT-KFQFREIEVETTEVK 199
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVN-DFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgCWTYGNLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPESIE--TRIVKHFHFTEWELDSFPYISafIELRRRVRQFMEKNPVEA-PMVVHCSNGAGRSGA 276
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGEkrVRLVTQFHFTSWPDFGVPFTP--IGMLKFLKKVKSANPPRAgPIVVHCSAGVGRTGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
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: 130.72 E-value: 1.20e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT---KFQFREIEVETTE 197
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVD-DFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMeegSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 198 VKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQFmeKNPVEAPMVVHCSNGAGRSGA 276
Cdd:cd14557   80 EKICPDYIIRKLNINNKK-EKGSGREVTHIQFTSWPDHGVPEdPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 131.87 E-value: 2.98e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  58 QERRKKRILFKGEYlmvnrsidnnKCRCDVGSTM--MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKA 135
Cdd:cd14603    5 SEIRACSAAFKADY----------VCSTVAGGRKenVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 136 YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKfqfreievettEVKTYSHFVIRTFKLT 212
Cdd:cd14603   75 YIATQG----PLSHtvlDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQ-----------EPLQTGPFTITLVKEK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 213 RTTPESI----------ETRIVKHFHFTEWE----LDSFPYISAFIELrrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFL 278
Cdd:cd14603  140 RLNEEVIlrtlkvtfqkESRSVSHFQYMAWPdhgiPDSPDCMLAMIEL---ARRLQGSGPE--PLCVHCSAGCGRTGVIC 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 212645549 279 ALD-ANLELMKKTGQLDF--FEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14603  215 TVDyVRQLLLTQRIPPDFsiFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264

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: 3.15e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  54 VAYVQE--RRKKRILFKGEYLMVNRSiDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGDENSHYINAS-YVNSW 130
Cdd:cd14609    4 LAYMEDhlRNRDRLAKEWQALCAYQA-EPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 131 LRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP---LTKFQFREIEVETTEVKTySHFVIR 207
Cdd:cd14609   83 PRMPAYIATQGPLSHTI-ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPdegSSLYHIYEVNLVSEHIWC-EDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 208 TFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLEL 286
Cdd:cd14609  161 SFYLKNV--QTQETRTLTQFHFLSWPAEGIPSSTrPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNR 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 212645549 287 MKK-TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14609  237 MAKgVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278

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: 1.07e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  92 MDRNPYPDTLPYDYNRVILPRIDGDENSHYINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14610   45 VQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLPATV-ADFWQMVWESGCVVIVMLTPLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPLTKFQFREI-EVETTEVKTYSH-FVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYIS-AFIELR 247
Cdd:cd14610  124 ENGVKQCYHYWPDEGSNLYHIyEVNLVSEHIWCEdFLVRSFYLKNL--QTNETRTVTQFHFLSWNDQGVPASTrSLLDFR 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 248 RRVRQFMEKNpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTG-QLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 326
Cdd:cd14610  202 RKVNKCYRGR--SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEE 279


                 .
gi 212645549 327 V 327
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: 129.12 E-value: 1.78e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDE-NSHYINASYVNSWL-------RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 165
Cdd:cd14544    4 KNRYKNILPFDHTRVILKDRDPNVpGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVS-DFWSMVWQENSRVIVM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 166 LTKVFDFMRVMCLQYWP--LTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETRIVKHFHFTEWE---LDSFPY- 239
Cdd:cd14544   83 TTKEVERGKNKCVRYWPdeGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLD-QGDPIREIWHYQYLSWPdhgVPSDPGg 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 240 ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQY 316
Cdd:cd14544  162 VLNFLE---DVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQY 238


                 ....
gi 212645549 317 MFIY 320
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: 9.18e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPL-TKFQFREIEVETTEVK 199
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQG-PLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAdGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPES------IETRIVKHFHFTEWELDSFP-YISAFIELRRRVRQfmEKNPVEAPMVVHCSNGAG 272
Cdd:cd17668   80 VLAYYTVRNFTLRNTKIKKgsqkgrPSGRVVTQYHYTQWPDMGVPeYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212645549 273 RSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
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: 124.79 E-value: 1.53e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKA--YVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP----LTKFQFREI 191
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQG----PLpntTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnKPLICGGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 192 EVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPyiSAFIELRRRVRqFMEKNPVEAPMVVHCSNGA 271
Cdd:cd14538   77 EVSLEKYQSLQDFVIRRISLRDK--ETGEVHHITHLNFTTWPDHGTP--QSADPLLRFIR-YMRRIHNSGPIVVHCSAGI 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 212645549 272 GRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEA 326
Cdd:cd14538  152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206

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

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 125.33 E-value: 2.23e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NL 461
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGvEGSDY--INASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVmltKL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 462 SNQGSQRHYPSFIHNKGkANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVRMWP 541
Cdd:cd14554   84 REMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFTDWP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 542 iENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 621
Cdd:cd14554  147 -EQGVPKSGEGFIDFIGQVH---KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPA 222

                        250
                 ....*....|..
gi 212645549 622 LIDMKDEYKYLY 633
Cdd:cd14554  223 MVQTEDQYQFCY 234

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

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 126.13 E-value: 2.29e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRID-GDENSHYINASYVNSW-LRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFD 171
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQG-PTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 172 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 250
Cdd:cd14613  107 -MNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG----EERGLKHYWYTSWPDQKTPdNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645549 251 RQFMEK-NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 324
Cdd:cd14613  182 EEARQQaEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLS 256

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: 124.95 E-value: 2.95e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQG----PLSttlLDFWRMIWEYSVLIIVMACMEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPLT---KFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIEL 246
Cdd:cd14602   77 EMGKKKCERYWAEPgemQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS----ETRTIYQFHYKNWPDHDVPsSIDPILEL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 247 RRRVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14602  153 IWDVRCYQEDDSV--PICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230


                 ..
gi 212645549 324 SE 325
Cdd:cd14602  231 IE 232

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: 3.06e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  92 MDRNPYPDTLPYDYNRVILpridgDENSHYINASYVNSWLrDKAYVVTQAVRTK-PMN---AEFWRMVWELGSNCIVMLT 167
Cdd:cd14600   41 MDKNRYKDVLPYDATRVVL-----QGNEDYINASYVNMEI-PSANIVNKYIATQgPLPhtcAQFWQVVWEQKLSLIVMLT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 168 KVFDFMRVMCLQYWPltkfqfreievETTEVKTYSHF-------------VIRTFKLTRTtpESIETRIVKHFHFTEWEL 234
Cdd:cd14600  115 TLTERGRTKCHQYWP-----------DPPDVMEYGGFrvqchsedctiayVFREMLLTNT--QTGEERTVTHLQYVAWPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 235 DSFPYISA-FIELRRRVRQFMEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSV 313
Cdd:cd14600  182 HGVPDDSSdFLEFVNYVRSKRVEN---EPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258

                        250
                 ....*....|
gi 212645549 314 EQYMFIYEVL 323
Cdd:cd14600  259 SQYKFVCEAI 268

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: 4.85e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR 174
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTV-GDFWRMVWETRAKTIVMLTQCFEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 175 VMCLQYWPLTKFQ---FREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFPYISA----FIELR 247
Cdd:cd14616   80 IRCHQYWPEDNKPvtvFGDIVITKLMEDVQIDWTIRDLKIERHG----DYMMVRQCNFTSWPEHGVPESSAplihFVKLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 248 RRVRQfmEKNpveAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
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: 6.77e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWP-LTKFQFREIEVETTEVK 199
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTV-ADFWRLVFDYNCSSVVMLNEM-DAAQ-LCMQYWPeKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 276
Cdd:cd14634   78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAyrDTPPSKRSILKVVRRLEKWQEQyDGREGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14634  158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 125.11 E-value: 1.48e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  50 ASKFVAYVQERRKKRILfKGEYLMVNRSIDNNKCRCDVGSTMMDRNPYPDTLPYDYNRVILPRIDGdeNSHYINASYVNS 129
Cdd:PHA02742  12 AKNCEQLIEESNLAEIL-KEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 130 WLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVI 206
Cdd:PHA02742  89 HNAKGRFICTQAPLEETAL-DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 207 RTFKLTRT-TPESIEtriVKHFHFTEWELDSFPY-ISAFIELRRRVRQFMEKNPV---------EAPMVVHCSNGAGRSG 275
Cdd:PHA02742 168 TNLCLTDTnTGASLD---IKHFAYEDWPHGGLPRdPNKFLDFVLAVREADLKADVdikgenivkEPPILVHCSAGLDRAG 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 212645549 276 AFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
Cdd:PHA02742 245 AFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289

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

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 123.54 E-value: 1.94e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDenshYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:cd14607   27 RNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQG----PLPntcCHFWLMVWQQKTKAVVMLNRIV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFMRVMCLQYWPLTK---FQFRE----IEVETTEVKTYshFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA- 242
Cdd:cd14607   99 EKDSVKCAQYWPTDEeevLSFKEtgfsVKLLSEDVKSY--YTVHLLQLENI--NSGETRTISHFHYTTWPDFGVPESPAs 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 243 FIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDfFEYAKTLVNSRPH---LIDSVEQYMFI 319
Cdd:cd14607  175 FLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDS-VDIKQVLLDMRKYrmgLIQTPDQLRFS 253


                 .
gi 212645549 320 Y 320
Cdd:cd14607  254 Y 254

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 120.02 E-value: 1.34e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVIL-PRIDGDENSHYINASYVNSWL-RDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFD 171
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVN-DFWQMVWQEDSPVIVMITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 172 fMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWELDSFP-YISAFIELRRRV 250
Cdd:cd14611   81 -KNEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS----QSRSVKHYWYTSWPDHKTPdSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 251 RQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
Cdd:cd14611  156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

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: 119.56 E-value: 3.24e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDG-DENSHYINASYVNSWL-RDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTK 168
Cdd:cd14612   18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQG----PMLntvSDFWEMVWQEECPIIVMITK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 169 VFDfMRVMCLQYWPLTKFQFREIEVETTEVKTYSHFVIRTFkltrTTPESIETRIVKHFHFTEWELDSFPYIS-AFIELR 247
Cdd:cd14612   94 LKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDL----TIQLEEESRSVKHYWFSSWPDHQTPESAgPLLRLV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 248 RRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLS 324
Cdd:cd14612  169 AEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLA 245

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: 118.59 E-value: 3.24e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVN-----SWLRDKaYVVTQAvrtkPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFRE 190
Cdd:cd14541    2 YINANYVNmeipgSGIVNR-YIAAQG----PLpntCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLgeTMQFGN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 191 IEVETTEVKTYSHFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQFmEKNPVEaPMVVHCSN 269
Cdd:cd14541   77 LQITCVSEEVTPSFAFREFILTNT--NTGEERHITQMQYLAWPDHGVPDDSSdFLDFVKRVRQN-RVGMVE-PTVVHCSA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645549 270 GAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14541  153 GIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCE 204

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: 6.06e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILpridGDENShYINASYVNSWLRDKAYVVTQAVRTKPMN-AEFWRMVWELGSNCIVMLTKVFDF 172
Cdd:cd14597    6 KNRYKNILPYDTTRVPL----GDEGG-YINASFIKMPVGDEEFVYIACQGPLPTTvADFWQMVWEQKSTVIAMMTQEVEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 173 MRVMCLQYWP--LTKFQFREIEVETTEVKT--YSHFVIRTFKLTRTtpESIETRIVKHFHFTEW---ELDSFPY-ISAFI 244
Cdd:cd14597   81 GKIKCQRYWPeiLGKTTMVDNRLQLTLVRMqqLKNFVIRVLELEDI--QTREVRHITHLNFTAWpdhDTPSQPEqLLTFI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212645549 245 ELRRRVRQfmeknpvEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
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: 117.16 E-value: 7.51e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYV-NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIeVETTEVK 199
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTI-ADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI-YEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYS---HFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPY-ISAFIELRRRV-RQFMEKNpveAPMVVHCSNGAGRS 274
Cdd:cd14546   79 EHIwcdDYLVRSFYLKNL--QTSETRTVTQFHFLSWPDEGIPAsAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645549 275 GAFLALDANLE-LMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14546  154 GTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207

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: 117.81 E-value: 1.65e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  93 DRNPYPDTLPYDYNRVILPriDGDEN---SHYINASYV---------NSWLRdKAYVVTQAVRTKPMNaEFWRMVWELGS 160
Cdd:cd14605    4 NKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIImpefetkcnNSKPK-KSYIATQGCLQNTVN-DFWRMVFQENS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 161 NCIVMLTKVFDFMRVMCLQYWPlTKFQFRE---IEVETTEVKTYSHFVIRTFKLTRTTPESIEtRIVKHFHFTEWELDSF 237
Cdd:cd14605   80 RVIVMTTKEVERGKSKCVKYWP-DEYALKEygvMRVRNVKESAAHDYILRELKLSKVGQGNTE-RTVWQYHFRTWPDHGV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 238 PY-ISAFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSV 313
Cdd:cd14605  158 PSdPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTE 237


                 ....*..
gi 212645549 314 EQYMFIY 320
Cdd:cd14605  238 AQYRFIY 244

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: 1.67e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKA--YVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQFREIEVETTEV 198
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTID-DFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 199 KTYS---HFVIRTFKLTRTtpESIETRIVKHFHFTEWELDSFPYISA----FIELRRRVRQfmeknpvEAPMVVHCSNGA 271
Cdd:cd14596   80 ENYQalqYFIIRIIKLVEK--ETGENRLIKHLQFTTWPDHGTPQSSDqlvkFICYMRKVHN-------TGPIVVHCSAGI 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 272 GRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAV 327
Cdd:cd14596  151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

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

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 115.39 E-value: 2.86e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTqavrTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVM-CLQYWPLTKFQ-FREIEVET 195
Cdd:cd14637    1 YINAALTDSYTRSAAFIVT----LHPLQnttTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPEPGLQqYGPMEVEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 196 TEVKTYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEKNPvEAPMVVHCSNGAGR 273
Cdd:cd14637   77 VSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAyrDTPDSKKAFLHLLASVEKWQRESG-EGRTVVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212645549 274 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 5.41e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTK---FQFREIEVETTE 197
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVL-DFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeeqLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 198 VKTYSH-FVIRTFKLTRTTpesiETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEKNPVeaPMVVHCSNGAGRSG 275
Cdd:cd14542   80 EKRVGPdFLIRTLKVTFQK----ESRTVYQFHYTAWpDHGVPSSVDPILDLVRLVRDYQGSEDV--PICVHCSAGCGRTG 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 212645549 276 AFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIY 320
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: 1.03e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWP-----LTKFQFRE 190
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQG----PLQNtvgDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 191 IEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEW-------ELDSF-PYISAFIELRRRVRQFMEKNPVEAP 262
Cdd:cd14540   77 YKVSTKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWpdhgcpeDVSGFlDFLEEINSVRRHTNQDVAGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645549 263 MVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
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: 2.06e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 395 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGSQR--H 469
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcmeKGRVKcdH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 470 YPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDImatgaqnqqidAEVRICCVIQVRMWPiENKVPLS 549
Cdd:cd14548   84 YWPF--DQDPVYYGDITVTMLSESVLPDWT-------IREFKLERG-----------DEVRSVRQFHFTAWP-DHGVPEA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 550 TTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEY 629
Cdd:cd14548  143 PDSLLRFVRLVRDYIKQ-----EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQY 217


                 ....
gi 212645549 630 KYLY 633
Cdd:cd14548  218 IFLH 221

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 115.41 E-value: 3.77e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  95 NPYPDTLPYDYNRVILP--RIDGDenshYINASYVNSWLRDKAYVVTQAvRTKPMNAEFWRMVWELGSNCIVMLTKVFDF 172
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPaeRNRGD----YINANYVDGFEYKKKFICGQA-PTRQTCYDFYRMLWMEHVQIIVMLCKKKEN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 173 MRVMCLQYW---PLTKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpESIETriVKHFHFTEWELDSFP-----YISAFI 244
Cdd:PHA02738 128 GREKCFPYWsdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQT--VTHFNFTAWPDHDVPkntseFLNFVL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 245 ELRRRVRQFME-------KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 317
Cdd:PHA02738 205 EVRQCQKELAQeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                 ....*.
gi 212645549 318 FIYEVL 323
Cdd:PHA02738 285 FCYRAV 290

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 114.33 E-value: 8.36e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILpRIDGDENSHYINASYVNSWLRDKAYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVF 170
Cdd:PHA02747  54 KNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQG----PFAetcADFWKAVWQEHCSIIVMLTPTK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 171 DFM-RVMCLQYWPLTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTpeSIETRIVKHFHFTEWELDSFP----YISA 242
Cdd:PHA02747 129 GTNgEEKCYQYWCLNEdgnIDMEDFRIETLKTSVRAKYILTLIEITDKI--LKDSRKISHFQCSEWFEDETPsdhpDFIK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 243 FIELRRRVRQ-----FMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYM 317
Cdd:PHA02747 207 FIKIIDINRKksgklFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                 ....*....
gi 212645549 318 FI---YEVL 323
Cdd:PHA02747 287 FIqpgYEVL 295

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 107.06 E-value: 1.48e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   223 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 300
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 212645549   301 TLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 107.06 E-value: 1.48e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   223 IVKHFHFTEWELDSFPYIS-AFIELRRRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLE-LMKKTGQLDFFEYAK 300
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPdSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQqLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 212645549   301 TLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 1.55e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVfDFMRvMCLQYWPLT-KFQFREIEVETTEVK 199
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVK-DFWRLVYDYGCTSIVMLNEV-DLAQ-GCPQYWPEEgMLRYGPIQVECMSCS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWELDSFPYIS--AFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 276
Cdd:cd14636   78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSkrSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSGM 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
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: 112.33 E-value: 3.26e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFM 173
Cdd:cd14604   60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTV-IDFWRMIWEYNVAIIVMACREFEMG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 174 RVMCLQYWPL---TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTpesiETRIVKHFHFTEWE----LDSFPYISAFIEL 246
Cdd:cd14604  139 RKKCERYWPLygeEPMTFGPFRISCEAEQARTDYFIRTLLLEFQN----ETRRLYQFHYVNWPdhdvPSSFDSILDMISL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 247 rrrVRQFMEKNPVeaPMVVHCSNGAGRSGAFLALDANLELMKK---TGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14604  215 ---MRKYQEHEDV--PICIHCSAGCGRTGAICAIDYTWNLLKAgkiPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289


                 ..
gi 212645549 324 SE 325
Cdd:cd14604  290 AQ 291

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350484 [Multi-domain] Cd Length: 206 Bit Score: 108.19 E-value: 1.11e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 496
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 497 amTSHMVKVMKRTFMISDImatgAQNQQIDAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 576
Cdd:cd14636   76 --CSMDCDVISRIFRICNL----TRPQEGYLMVQ---QFQYLGWASHREVPGSKRSFLKLILQVEKWQEEC-DEGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645549 577 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14636  145 IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 107.08 E-value: 2.66e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMrvMCLQYWPLTKF-QFREIEVETTEVK 199
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVK-DFWRLVLDYHCTSIVMLNDVDPAQ--LCPQYWPENGVhRHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 200 TYSHFVIRTFKLTRTTPESIETRIVKHFHFTEWEL--DSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCSNGAGRSGA 276
Cdd:cd14635   78 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMyrDTPVSKRSFLKLIRQVDKWQEEyNGGEGRTVVHCLNGGGRSGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645549 277 FLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSE 325
Cdd:cd14635  158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

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: 109.05 E-value: 4.26e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 463
Cdd:cd14627   53 NKFKNRLVNIMPYETTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 538
Cdd:cd14627  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 539 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 618
Cdd:cd14627  191 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 212645549 619 RPQLIDMKDEYKYLYDVMLHW 639
Cdd:cd14627  267 RPAMVQTEDEYQFCYQAALEY 287

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: 109.05 E-value: 4.32e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 463
Cdd:cd14628   52 NKFKNRLVNIMPYESTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 538
Cdd:cd14628  130 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTVRQFQFT 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 539 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 618
Cdd:cd14628  190 DWP-EQGVPKSGEGFIDFIGQVHKTKEQFG---QDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265

                        250       260
                 ....*....|....*....|.
gi 212645549 619 RPQLIDMKDEYKYLYDVMLHW 639
Cdd:cd14628  266 RPAMVQTEDQYQFCYRAALEY 286

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 106.31 E-value: 4.64e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYP 496
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 497 AMTSHMVKVMkrtfmisdimaTGAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 576
Cdd:cd14635   81 DIISRIFRIY-----------NAARPQD---GYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEY-NGGEGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645549 577 IVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14635  145 VVHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205

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: 2.51e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQgSQRHYPSFIH--NKGKANYGPFIVEIMNy 492
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQ-SNSAWPCLQYwpEPGLQQYGPMEVEFVS- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 493 hqypamTSHMVKVMKRTFMISDImaTGAQNQQIdaevrICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRAPDrpe 572
Cdd:cd14637   79 ------GSADEDIVTRLFRVQNI--TRLQEGHL-----MVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGE--- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212645549 573 tKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
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: 105.35 E-value: 4.38e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  94 RNPYPDTLPYDYNRVILPriDGDEN---SHYINASYVNS--WLRD---KAYVVTQAVRTKPMNaEFWRMVWELGSNCIVM 165
Cdd:cd14606   21 KNRYKNILPFDHSRVILQ--GRDSNipgSDYINANYVKNqlLGPDenaKTYIASQGCLEATVN-DFWQMAWQENSRVIVM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 166 LTKVFDFMRVMCLQYWPLTKFQ--FREIEVETTEVKTYSHFVIRTFKLtrTTPESIET-RIVKHFHFTEWELDSFPY--- 239
Cdd:cd14606   98 TTREVEKGRNKCVPYWPEVGMQraYGPYSVTNCGEHDTTEYKLRTLQV--SPLDNGELiREIWHYQYLSWPDHGVPSepg 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 240 -ISAFIElrrRVRQFMEKNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTG---QLDFFEYAKTLVNSRPHLIDSVEQ 315
Cdd:cd14606  176 gVLSFLD---QINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQ 252


                 ....*
gi 212645549 316 YMFIY 320
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: 3.54e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNyhqyp 496
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVS----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 497 amTSHMVKVMKRTFMISDImatgAQNQQidaEVRICCVIQVRMWPIENKVPLSTTGLIDVIKMARSWRKRApDRPETKpT 576
Cdd:cd14634   76 --ADIDEDIISRIFRICNM----ARPQD---GYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQY-DGREGR-T 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 577 IVMSHNGVSRVGVYIG-ANIC--IDQMDIdheVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
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: 99.69 E-value: 8.55e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPSfihnKGKANYGPFIVEIM 490
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTelqereQEKCVQYWPS----EGSVTHGEITIEIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 491 NyhqypamtshmvKVMKRTFMISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR 570
Cdd:cd14622   78 N------------DTLLETISIRDFLVTYNQEKQ----TRLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQTGNH 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 571 petkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 636
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: 1.24e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINAS----YVNSWLRdkaYVVTQAvrtkPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLTKFQ---FRE 190
Cdd:cd14539    1 YINASliedLTPYCPR---FIATQA----PLPgtaADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQalvYGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 191 IEVETTEVKTYSHFVIRTFKLTrtTPESIETRIVKHFHFTEW-ELDSFPYISAFIELRRRVRQFMEK-NPVEAPMVVHCS 268
Cdd:cd14539   74 ITVSLQSVRTTPTHVERIISIQ--HKDTRLSRSVVHLQFTTWpELGLPDSPNPLLRFIEEVHSHYLQqRSLQTPIVVHCS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645549 269 NGAGRSGAF-LALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
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: 100.57 E-value: 2.74e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHG-ESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN- 463
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQPIRGvEGSDY--INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKl 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 -----QGSQRHYPSfihnKGKANYGPFIVEIMNYHQYPamtshmvKVMKRTFMISDIMatgaqnqqiDAEVRICCVIQVR 538
Cdd:cd14629  131 remgrEKCHQYWPA----ERSARYQYFVVDPMAEYNMP-------QYILREFKVTDAR---------DGQSRTIRQFQFT 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 539 MWPiENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 618
Cdd:cd14629  191 DWP-EQGVPKTGEGFIDFIGQVHKTKEQFG---QDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266

                        250       260
                 ....*....|....*....|.
gi 212645549 619 RPQLIDMKDEYKYLYDVMLHW 639
Cdd:cd14629  267 RPAMVQTEDQYQLCYRAALEY 287

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 100.10 E-value: 6.52e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 103 YDYNRVILPRIDGDENshYINASYVNSWLRDKAYVVTQAVRtKPMNAEFWRMVWELGSNCIVMLTKVFDFMRVmCLQYWP 182
Cdd:PHA02746  84 SDGKKIEVTSEDNAEN--YIHANFVDGFKEANKFICAQGPK-EDTSEDFFKLISEHESQVIVSLTDIDDDDEK-CFELWT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 183 LTK---FQFREIEVETTEVKTYSHFVIRTFKLTRTTPESieTRIVKHFHFTEWELDSFPY-ISAFIELRRRV---RQFME 255
Cdd:PHA02746 160 KEEdseLAFGRFVAKILDIIEELSFTKTRLMITDKISDT--SREIHHFWFPDWPDNGIPTgMAEFLELINKVneeQAELI 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645549 256 KN-----PVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVLSEAVM 328
Cdd:PHA02746 238 KQadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315

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: 97.01 E-value: 6.97e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQavrtKPMN---AEFWRMVWELGSNCIVMLTKvfDFMRVMCLQYWPLtkfQFREIEVETTE 197
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQ----HPLEhtiKDFWQMIWDHNSQTIVMLTD--NELNEDEPIYWPT---KEKPLECETFK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 198 VK----------TYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPYISAFiELRRRVRQfmEKNPVEAPMVVHC 267
Cdd:cd14550   72 VTlsgedhsclsNEIRLIVRDFILESTQDDYVLE--VRQFQCPSWPNPCSPIHTVF-ELINTVQE--WAQQRDGPIVVHD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212645549 268 SNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYE 321
Cdd:cd14550  147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

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: 7.75e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 378 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHT 457
Cdd:cd14621   44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEG-VPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 458 VVNLSNQGSQRH--YPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVI 535
Cdd:cd14621  123 IVMVTNLKERKEckCAQYWPDQGCWTYGNIRVSVED-------VTVLVDYTVRKFCIQQVGDVTNKKPQ-----RLITQF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 536 QVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMM 615
Cdd:cd14621  191 HFTSWP-DFGVPFTPIGMLKFLK-----KVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRI 264

                        250       260
                 ....*....|....*....|....*.
gi 212645549 616 RINRPQLIDMKDEYKYLYDVMLHWYM 641
Cdd:cd14621  265 RAQRCQMVQTDMQYVFIYQALLEHYL 290

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 96.93 E-value: 1.33e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 395 VVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFI 474
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCS-DYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 475 H--NKGKANYGPFIVEIMNYhqypamtSHMVKVMKRTFMISDIMATGAQNQqidaevRICCVIQVRMWPiENKVPLSTTG 552
Cdd:cd14620   83 YwpDQGCWTYGNIRVAVEDC-------VVLVDYTIRKFCIQPQLPDGCKAP------RLVTQLHFTSWP-DFGVPFTPIG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 553 LIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYL 632
Cdd:cd14620  149 MLKFLKKVKSV-----NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFI 223


                 ....*
gi 212645549 633 YDVML 637
Cdd:cd14620  224 YQALL 228

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: 1.65e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 390 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS---NQGS 466
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHS-DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 467 ---QRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDAEVRICcVIQVRMWPiE 543
Cdd:cd14618   80 vlcDHYWPS---ESTPVSYGHITVHLLAQSSEDEWT-------RREFKL--------WHEDLRKERRVK-HLHYTAWP-D 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 544 NKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 623
Cdd:cd14618  140 HGIPESTSSLMAFRELVREHVQATKGK---GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMI 216

                        250
                 ....*....|....
gi 212645549 624 DMKDEYKYLYDVML 637
Cdd:cd14618  217 QTLSQYIFLHSCIL 230

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 95.01 E-value: 5.04e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMN---AEFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPLT--KFQFREIEVET 195
Cdd:cd14601    2 YINANYINMEIPSSSIINRYIACQGPLPntcSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPsgSSSYGGFQVTC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 196 TEVKTYSHFVIRtfKLTRTTPESIETRIVKHFHFTEWELDSFPYISA-FIELRRRVRQfmEKNPVEAPMVVHCSNGAGRS 274
Cdd:cd14601   82 HSEEGNPAYVFR--EMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 212645549 275 GAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
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: 8.00e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQ 494
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTeiKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 YPAMTshmvkvmkrtfmISDIMATGAQNQQidaeVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDRPETk 574
Cdd:cd14552   81 YEDYT------------LRDFLVTKGKGGS----TRTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQSGNHPIT- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212645549 575 ptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 636
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: 1.85e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549  93 DRNPYPDTLPYDYNRV-ILPriDGDENSHYINASYVNSWLRDKA--YVVTQAvrtkPMN---AEFWRMVWELGSNCIVML 166
Cdd:cd14599   40 ERNRIREVVPYEENRVeLVP--TKENNTGYINASHIKVTVGGEEwhYIATQG----PLPhtcHDFWQMVWEQGVNVIAMV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 167 TKVFDFMRVMCLQYWP----------------LTKFQFREIEVETTEVKTySHFVirtfkltrttpeSIETRIVKHFHFT 230
Cdd:cd14599  114 TAEEEGGRSKSHRYWPklgskhssatygkfkvTTKFRTDSGCYATTGLKV-KHLL------------SGQERTVWHLQYT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 231 EW-------ELDSF-PYISAFIELRRRVRQFME-KNPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKT 301
Cdd:cd14599  181 DWpdhgcpeEVQGFlSYLEEIQSVRRHTNSMLDsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRH 260

                        250       260
                 ....*....|....*....|..
gi 212645549 302 LVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14599  261 LREQRMFMIQTIAQYKFVYQVL 282

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 92.46 E-value: 2.74e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQR---HYpsfiHNKGKANYGPFIVEIMN 491
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElkEGDQEqcaQY----WGDEKKTYGDIEVELKD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 492 YHQYPAMTshmvkvmKRTFMIsdimatgaQNQQIDaEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDR- 570
Cdd:cd14558   77 TEKSPTYT-------VRVFEI--------THLKRK-DSRTVYQYQYHKWK-GEELPEKPKDLVDMIKSIKQKLPYKNSKh 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 571 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 634
Cdd:cd14558  140 GRSVPIVVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350478 [Multi-domain] Cd Length: 237 Bit Score: 93.17 E-value: 3.12e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ 464
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHS-DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 465 ------GSQRHYPSfihnkGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdimatgaqNQQIDAEVRICCVIQVR 538
Cdd:cd14630   81 vevgrvKCVRYWPD-----DTEVYGDIKVTLIE-------TEPLAEYVIRTFTV---------QKKGYHEIREIRQFHFT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 539 MWPiENKVPLSTTGLIDVIKMARSWrkrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRIN 618
Cdd:cd14630  140 SWP-DHGVPCYATGLLGFVRQVKFL-----NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQ 213

                        250
                 ....*....|....*....
gi 212645549 619 RPQLIDMKDEYKYLYDVML 637
Cdd:cd14630  214 RVNMVQTEEQYVFVHDAIL 232

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 91.52 E-value: 1.01e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 390 NRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVnLSNQGSQR- 468
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCS-DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIV-MVTQCVEKg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 469 -----HYPSFIHNKgkANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatgaqNQQIDAEvRICCVIQVRMWPiE 543
Cdd:cd14617   79 rvkcdHYWPADQDS--LYYGDLIVQMLSESVLPEWTI-------REFKICS-------EEQLDAP-RLVRHFHYTVWP-D 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 544 NKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 623
Cdd:cd14617  141 HGVPETTQSLIQFVRTVRDYINRTPG---SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMV 217

                        250
                 ....*....|
gi 212645549 624 DMKDEYKYLY 633
Cdd:cd14617  218 QTECQYVYLH 227

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

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 91.25 E-value: 3.49e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHG-ESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN 463
Cdd:cd17667   26 DNKHKNRYINILAYDHSRVKLRPLPGkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 --QGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMATGAQNQQIDAEVRICCVIQVR--M 539
Cdd:cd17667  106 lvEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTV-------RRFSIRNTKVKKGQKGNPKGRQNERTVIQYHytQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 540 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINR 619
Cdd:cd17667  179 WP-DMGVPEYALPVLTFVR-----RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                        250
                 ....*....|....*...
gi 212645549 620 PQLIDMKDEYKYLYDVML 637
Cdd:cd17667  253 NYLVQTEEQYIFIHDALL 270

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: 3.83e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 390 NRDVMVVPPDHARPYLQTLHgESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQ 467
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIH-EEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNcmEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 468 ---RHYPSFihNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDIMatgaqnQQIDAEVRiccVIQVRMWPiEN 544
Cdd:cd14619   80 vkcEHYWPL--DYTPCTYGHLRVTVVSEEVMENWTV-------REFLLKQVE------EQKTLSVR---HFHFTAWP-DH 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 545 KVPLSTTGLIDVIKMARSWRKRapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 624
Cdd:cd14619  141 GVPSSTDTLLAFRRLLRQWLDQ---TMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQ 217

                        250
                 ....*....|...
gi 212645549 625 MKDEYKYLYDVML 637
Cdd:cd14619  218 TESQYVFLHQCIL 230

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: 89.11 E-value: 6.25e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 390 NRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN---QGS 466
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDDY--INANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 467 ---QRHYPSfihnKGKANYGPFIVeimnyhqypAMTSHMVKvmkRTFMISDIMATGAQNQQIDaevricCVIQVRM--WP 541
Cdd:cd14615   79 tkcEEYWPS----KQKKDYGDITV---------TMTSEIVL---PEWTIRDFTVKNAQTNESR------TVRHFHFtsWP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 542 iENKVPLSTTGLIDVIKMARSWRKRAPdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQ 621
Cdd:cd14615  137 -DHGVPETTDLLINFRHLVREYMKQNP---PNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPL 212

                        250
                 ....*....|.
gi 212645549 622 LIDMKDEYKYL 632
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: 1.63e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGeSKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 465
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEG-VPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 466 SQ------RHYPsfihNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMIsdiMATGAQNQQidaEVRiccVIQVRM 539
Cdd:cd14553   82 ERsrvkcdQYWP----TRGTETYGLIQVTLLD-------TVELATYTVRTFAL---HKNGSSEKR---EVR---QFQFTA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 540 WPiENKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIganiCIDQM--DIDHE--VDVFHAVKMM 615
Cdd:cd14553  142 WP-DHGVPEHPTPFLAFLR-----RVKACNPPDAGPIVVHCSAGVGRTGCFI----VIDSMleRIKHEktVDIYGHVTCL 211

                        250       260
                 ....*....|....*....|..
gi 212645549 616 RINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14553  212 RAQRNYMVQTEDQYIFIHDALL 233

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: 3.64e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 464
Cdd:cd14633   39 ENRMKNRYGNIIAYDHSRVRLQPIEGETSS-DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 465 gsqrhypsfihnkgkanygpfIVEI--MNYHQYPAMTSHMVKVMKRTFMISDIMA-----TGAQNQQIDAEVRICCVIQV 537
Cdd:cd14633  117 ---------------------LVEVgrVKCCKYWPDDTEIYKDIKVTLIETELLAeyvirTFAVEKRGVHEIREIRQFHF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 538 RMWPiENKVPLSTTGLIDVIKMARSwrkRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRI 617
Cdd:cd14633  176 TGWP-DHGVPYHATGLLGFVRQVKS---KSP--PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRS 249

                        250       260
                 ....*....|....*....|
gi 212645549 618 NRPQLIDMKDEYKYLYDVML 637
Cdd:cd14633  250 RRVNMVQTEEQYVFIHDAIL 269

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: 4.20e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYV--NSWLRDKAYVVTQAVRTKPMnAEFWRMVWELGSNCIVMLTKVFDFMR-VMCLQYWPLTKFQFRE---IEVE 194
Cdd:cd17658    1 YINASLVetPASESLPKFIATQGPLPHTF-EDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREfgrISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 195 TTEVKTYSH-FVIRTFKLTRTtpESIET-RIVKHFHFTEWELDSFPYISAFI-ELRRRVRQFmekNPVEAPMVVHCSNGA 271
Cdd:cd17658   80 NKKLKHSQHsITLRVLEVQYI--ESEEPpLSVLHIQYPEWPDHGVPKDTRSVrELLKRLYGI---PPSAGPIVVHCSAGI 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212645549 272 GRSGAFLALDANLELMKKtGQLDFFEYAKTLVNSRPHLIDSV---EQYMFIYE 321
Cdd:cd17658  155 GRTGAYCTIHNTIRRILE-GDMSAVDLSKTVRKFRSQRIGMVqtqDQYIFCYA 206

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: 6.06e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKA--YVVTQAvrtkPMNA---EFWRMVWELGSNCIVMLTKVFDFMRVMCLQYWPltKFQFREIEVet 195
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQG----PLQNtcqDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWP--RLGSRHNTV-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 196 tevkTYSHFVIRT-FKLTR----TTPESI------ETRIVKHFHFTEWELDSFP--------YISAFIELRRRVRQFMEK 256
Cdd:cd14598   73 ----TYGRFKITTrFRTDSgcyaTTGLKIkhlltgQERTVWHLQYTDWPEHGCPedlkgflsYLEEIQSVRRHTNSTIDP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 257 NPVEAPMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd14598  149 KSPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215

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: 85.45 E-value: 6.35e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFIHNKGKA-NYGPFIVEIMNYHQY 495
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPlECETFKVTLSGEDHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 496 PAMTSHMVKVmkRTFMIsdimatgaQNQQID--AEVRIccvIQVRMWPIENKvPLSTT-GLIDVIkmarswRKRAPDRpe 572
Cdd:cd14550   81 CLSNEIRLIV--RDFIL--------ESTQDDyvLEVRQ---FQCPSWPNPCS-PIHTVfELINTV------QEWAQQR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212645549 573 TKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
Cdd:cd14550  139 DGPIVVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199

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

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 87.46 E-value: 7.14e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 463
Cdd:cd14625   47 NKPKNRYANVIAYDHSRVILQPIEGIMGS-DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTklE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFmisDIMATGAQNQQidaEVRiccVIQVRMWPiE 543
Cdd:cd14625  126 EKSRIKCDQYWPSRGTETYGMIQVTLLD-------TIELATFCVRTF---SLHKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 544 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 623
Cdd:cd14625  189 HGVPEYPTPFLAFLR-----RVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMV 263

                        250
                 ....*....|....
gi 212645549 624 DMKDEYKYLYDVML 637
Cdd:cd14625  264 QTEDQYSFIHDALL 277

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: 9.80e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 490
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLvevgrvKCSKYWP-----DDSDTYGDIKITLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 491 NyhqypamTSHMVKVMKRTFMISdimatgAQNQQIDAEVricCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 570
Cdd:cd14632   76 K-------TETLAEYSVRTFALE------RRGYSARHEV---KQFHFTSWP-EHGVPYHATGLLAFIR-----RVKASTP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 571 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14632  134 PDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

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

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 87.01 E-value: 1.04e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS--N 463
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGS-DYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTrlE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 543
Cdd:cd14626  120 EKSRVKCDQYWPIRGTETYGMIQVTLLD-------TVELATYSVRTFA---LYKNGSSEKR---EVR---QFQFMAWP-D 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 544 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 623
Cdd:cd14626  183 HGVPEYPTPILAFLR-----RVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMV 257

                        250
                 ....*....|....
gi 212645549 624 DMKDEYKYLYDVML 637
Cdd:cd14626  258 QTEDQYIFIHEALL 271

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: 84.73 E-value: 1.45e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL-SNQGSQR----HYPSfihNKGKANYGPFIVEIMN 491
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEdefvYWPS---REESMNCEAFTVTLIS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 492 yhqypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKVPLSTTGLIDVIKmarswrKRAPDRp 571
Cdd:cd17670   78 -------KDRLCLSNEEQIIIHDFILEATQDDYV-LEVR---HFQCPKWPNPDAPISSTFELINVIK------EEALTR- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 572 eTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd17670  140 -DGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 84.66 E-value: 1.52e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWP-------LTKFQFREIEV 193
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIK-DFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkdepinCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 194 ETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNGAGR 273
Cdd:cd17669   79 EHKCLSNEEKLIIQDFILEATQDDYVLE--VRHFQCPKWPNPDSP-ISKTFELISIIKE--EAANRDGPMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 212645549 274 SGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd17669  154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 83.81 E-value: 2.86e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVEIMNyhq 494
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNlkERKEKKCSQYWPDQGCWTYGNLRVRVED--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 ypamTSHMVKVMKRTFMISDIMATGAQNQQidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSwrkraPDRPETK 574
Cdd:cd14551   78 ----TVVLVDYTTRKFCIQKVNRGIGEKRV-----RLVTQFHFTSWP-DFGVPFTPIGMLKFLKKVKS-----ANPPRAG 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 212645549 575 PTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
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: 84.70 E-value: 5.29e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 378 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVE-VDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 456
Cdd:cd14609   34 CSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRS-DYINASPiIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 457 TVVNLSN------QGSQRHYPsfihNKGKANYGPFIVEIMNYHqypamtshmvkVMKRTFMISDIMATGAQNQqidaEVR 530
Cdd:cd14609  113 VIVMLTPlvedgvKQCDRYWP----DEGSSLYHIYEVNLVSEH-----------IWCEDFLVRSFYLKNVQTQ----ETR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 531 ICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDV 608
Cdd:cd14609  174 TLTQFHFLSWPAEG-IPSSTRPLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDI 246

                        250       260
                 ....*....|....*....|...
gi 212645549 609 FHAVKMMRINRPQLIDMKDEYKY 631
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: 8.77e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV---NLSNQGSQ---RHYPsfihNKGKANYGPFIVEIM 490
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVmitNLVERGRRkcdQYWP----KEGTETYGNIQVTLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 491 NyhqypamTSHMVKVMKRTFMISDimaTGAQNQQIDAEVRIccVIQVRM--WPiENKVPLSTTGLIDVIKmarswRKRAP 568
Cdd:cd14549   77 S-------TEVLATYTVRTFSLKN---LKLKKVKGRSSERV--VYQYHYtqWP-DHGVPDYTLPVLSFVR-----KSSAA 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 569 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYD 634
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: 5.09e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 381 GHRLENRGKNrdvmVVPPDHARPYLQTLHGESKDYTYINAVEVDGFT-RKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV 459
Cdd:cd14612   14 GHASKDRYKT----ILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 460 NLSNQGSQRHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTshmvkvmkrtfmISDIMAtgaqnqQIDAEVRICCVIQVRM 539
Cdd:cd14612   90 MITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYT------------IRDLTI------QLEEESRSVKHYWFSS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 540 WPiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINR 619
Cdd:cd14612  152 WP-DHQTPESAGPLLRLVAEVEESRQTAASP---GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDR 227

                        250
                 ....*....|....
gi 212645549 620 PQLIDMKDEYKYLY 633
Cdd:cd14612  228 GGMIQTSEQYQFLH 241

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 80.47 E-value: 6.95e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 391 RDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYD-HACHTVV--NLSNQGSQ 467
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGE-ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEwKSCSIVMltELEERGQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 468 R---HYPSfihnKGKANYGPFIVEIMNYHQypamtshmvkvmKRTFMISDIMATGAQNQQiDAEVRiccVIQVRMWPiEN 544
Cdd:cd14623   80 KcaqYWPS----DGSVSYGDITIELKKEEE------------CESYTVRDLLVTNTRENK-SRQIR---QFHFHGWP-EV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 545 KVPLSTTGLIDVIKMARSWRKRAPDRPETkptiVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 624
Cdd:cd14623  139 GIPSDGKGMINIIAAVQKQQQQSGNHPIT----VHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQ 214

                        250
                 ....*....|..
gi 212645549 625 MKDEYKYLYDVM 636
Cdd:cd14623  215 TLEQYEFCYKVV 226

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

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 78.81 E-value: 1.56e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPsfihnKGKANYGPFIVEIM 490
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLvevgrvKCSRYWP-----DDTEVYGDIKVTLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 491 NyhqypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDR 570
Cdd:cd14555   76 E-------TEPLAEYVVRTFALE---------RRGYHEIREVRQFHFTGWP-DHGVPYHATGLLGFIR-----RVKASNP 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 571 PETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14555  134 PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350506 [Multi-domain] Cd Length: 209 Bit Score: 78.87 E-value: 1.66e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGSQRHYPSFIHNKGKANYGPFIVeimnyhq 494
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlvEKGRRKCDQYWPADGSEEYGNFLV------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 ypamTSHMVKVMK----RTFMISDI-MATGAQNQQidAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRkrapd 569
Cdd:cd17668   74 ----TQKSVQVLAyytvRNFTLRNTkIKKGSQKGR--PSGRVVTQYHYTQWP-DMGVPEYTLPVLTFVRKASYAK----- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212645549 570 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd17668  142 RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

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

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 80.55 E-value: 1.76e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN-- 463
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGS-DYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKle 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 QGSQRHYPSFIHNKGKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMisdIMATGAQNQQidaEVRiccVIQVRMWPiE 543
Cdd:cd14624  126 ERSRVKCDQYWPSRGTETYGLIQVTLLD-------TVELATYCVRTFA---LYKNGSSEKR---EVR---QFQFTAWP-D 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 544 NKVPLSTTGLIDVIKmarswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLI 623
Cdd:cd14624  189 HGVPEHPTPFLAFLR-----RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMV 263

                        250
                 ....*....|....
gi 212645549 624 DMKDEYKYLYDVML 637
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: 2.45e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 378 CAGGHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDyTYINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 456
Cdd:cd14610   36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHS-DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 457 TVVNLS---NQGSQRHYpSFIHNKGKANYGPFIVEIMNYHQYPAmtshmvKVMKRTFMISDIMATgaqnqqidaEVRICC 533
Cdd:cd14610  115 VIVMLTplaENGVKQCY-HYWPDEGSNLYHIYEVNLVSEHIWCE------DFLVRSFYLKNLQTN---------ETRTVT 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 534 VIQVRMWpIENKVPLSTTGLIDV-IKMARSWRKRapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHA 611
Cdd:cd14610  179 QFHFLSW-NDQGVPASTRSLLDFrRKVNKCYRGR------SCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAAT 251

                        250       260
                 ....*....|....*....|
gi 212645549 612 VKMMRINRPQLIDMKDEYKY 631
Cdd:cd14610  252 LEHLRDQRPGMVQTKEQFEF 271

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: 77.80 E-value: 3.21e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 121 YINASYVNSWLRDKAYVVTQavrtKPM---NAEFWRMVWELGSNCIVMLTKVFDFMRVMCLqYWPLTK-------FQFRE 190
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQ----HPLphtTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPSREesmnceaFTVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 191 IEVETTEVKTYSHFVIRTFKLTRTTPESIETriVKHFHFTEWELDSFPyISAFIELRRRVRQfmEKNPVEAPMVVHCSNG 270
Cdd:cd17670   76 ISKDRLCLSNEEQIIIHDFILEATQDDYVLE--VRHFQCPKWPNPDAP-ISSTFELINVIKE--EALTRDGPTIVHDEFG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212645549 271 AGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:cd17670  151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

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 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH--ACHTVV-NLSNQGSQRHYPSFIHNkgKANYGPFIVEIMNyh 493
Cdd:cd14631   15 YINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEqsACIVMVtNLVEVGRVKCYKYWPDD--TEVYGDFKVTCVE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 494 qypamTSHMVKVMKRTFMISdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKmarswRKRAPDRPET 573
Cdd:cd14631   91 -----MEPLAEYVVRTFTLE---------RRGYNEIREVKQFHFTGWP-DHGVPYHATGLLSFIR-----RVKLSNPPSA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 574 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
Cdd:cd14631  151 GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

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: 7.18e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   540 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 618
Cdd:smart00012  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 212645549   619 RPQLIDMKDEYKYLYDVMLH 638
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: 7.18e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549   540 WPiENKVPLSTTGLIDVIKMARSWRKrapDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD-IDHEVDVFHAVKMMRIN 618
Cdd:smart00404  10 WP-DHGVPESPDSILELLRAVKKNLN---QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEaEAGEVDIFDTVKELRSQ 85

                           90       100
                   ....*....|....*....|
gi 212645549   619 RPQLIDMKDEYKYLYDVMLH 638
Cdd:smart00404  86 RPGMVQTEEQYLFLYRALLE 105

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 76.57 E-value: 9.70e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-NQGSQRHYPSFIHNKGKA-NYGPFIVEIMNyhq 494
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdGQNMAEDEFVYWPNKDEPiNCETFKVTLIA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 ypamTSHMVKVMKRTFMISDIMATGAQNQQIdAEVRiccVIQVRMWPIENKvPLSTT-GLIDVIKMARSWRKrapdrpet 573
Cdd:cd17669   78 ----EEHKCLSNEEKLIIQDFILEATQDDYV-LEVR---HFQCPKWPNPDS-PISKTfELISIIKEEAANRD-------- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 574 KPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
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: 4.23e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGEsKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG 465
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEE-EGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 466 SQR-----HYPSFihNKGKANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdiMATGAQnqqidaevricCVIQVRM- 539
Cdd:cd14614   91 EKRrvkcdHYWPF--TEEPVAYGDITVEMLSEEEQPDWA-------IREFRVS--YADEVQ-----------DVMHFNYt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 540 -WPiENKVPLSTTG--LIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGVYIGANiCIDQMDIDHE-VDVFHAVKMM 615
Cdd:cd14614  149 aWP-DHGVPTANAAesILQFVQMVRQQAVKSKG-----PMIIHCSAGVGRTGTFIALD-RLLQHIRDHEfVDILGLVSEM 221

                        250
                 ....*....|....*...
gi 212645549 616 RINRPQLIDMKDEYKYLY 633
Cdd:cd14614  222 RSYRMSMVQTEEQYIFIH 239

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 75.04 E-value: 1.66e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 462
Cdd:PHA02747  50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDY--IHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpt 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 --NQGSQRHYPSFIHNK-GKANYGPFIVEIMNyhqypamTSHMVKVMKRTFMISDimatgaqnqQIDAEVRICCVIQVRM 539
Cdd:PHA02747 128 kgTNGEEKCYQYWCLNEdGNIDMEDFRIETLK-------TSVRAKYILTLIEITD---------KILKDSRKISHFQCSE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 540 WPIENkVPLSTTGLIDVIKMARSWRKRA-----PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 614
Cdd:PHA02747 192 WFEDE-TPSDHPDFIKFIKIIDINRKKSgklfnPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                        250       260
                 ....*....|....*....|....*..
gi 212645549 615 MRINRPQLIDMKDEYKYL---YDVMLH 638
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: 73.51 E-value: 2.10e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA--------VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACH 456
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINAniimpefeTKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 457 TVVnLSNQGSQRhypsfihnkGKANYGPFIVEIMNYHQYPAMTSHMVK-VMKRTFMISDIMAT--GAQNQQidaevRICC 533
Cdd:cd14605   81 VIV-MTTKEVER---------GKSKCVKYWPDEYALKEYGVMRVRNVKeSAAHDYILRELKLSkvGQGNTE-----RTVW 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 534 VIQVRMWPiENKVPLSTTGLIDVIKMARswrKRAPDRPETKPTIVMSHNGVSRVGVYIGANICID---QMDIDHEVDVFH 610
Cdd:cd14605  146 QYHFRTWP-DHGVPSDPGGVLDFLEEVH---HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDiirEKGVDCDIDVPK 221

                        250       260       270
                 ....*....|....*....|....*....|..
gi 212645549 611 AVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 642
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: 73.32 E-value: 3.57e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 381 GHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDH------- 453
Cdd:cd14603   25 GGRKENVKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYgvkvilm 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 454 ACHTVVNlSNQGSQRHYPSfihNKGKANYGPFIVEIMNYHQYPAMTshMVKVMKRTFmisdimatgaqnQQidaEVRICC 533
Cdd:cd14603  104 ACREIEM-GKKKCERYWAQ---EQEPLQTGPFTITLVKEKRLNEEV--ILRTLKVTF------------QK---ESRSVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 534 VIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRAPDrpetkPTIVMSHNGVSRVGV-----YIgANICIDQMdIDHEVDV 608
Cdd:cd14603  163 HFQYMAWP-DHGIPDSPDCMLAMIELARRLQGSGPE-----PLCVHCSAGCGRTGVictvdYV-RQLLLTQR-IPPDFSI 234

                        250       260
                 ....*....|....*....|....*
gi 212645549 609 FHAVKMMRINRPQLIDMKDEYKYLY 633
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: 4.39e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-------NQGSQrHYPSFihNKGKANYGPFIVEI 489
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrceegnrNKCAQ-YWPSM--EEGSRAFGDVVVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 490 MNYHQYPamtshmvKVMKRTFMISdimatgaqNQQIDAEVRICCVIQVRMWPiENKVPLSTTGLidvIKMARswRKRAPD 569
Cdd:cd14557   78 NEEKICP-------DYIIRKLNIN--------NKKEKGSGREVTHIQFTSWP-DHGVPEDPHLL---LKLRR--RVNAFN 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 570 RPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
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: 72.78 E-value: 6.14e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNR--DVMVVppDHARPYLQTLHGEskDYT-YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 462
Cdd:cd14543   29 NQEKNRygDVLCL--DQSRVKLPKRNGD--ERTdYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 N--QGSQRHYPSFIHNKGKA--NYGPFIV---EIMNYHQYpamtshmvkvMKRTFMIsdimatgaQNQQIDaEVRicCVI 535
Cdd:cd14543  105 RvvERGRVKCGQYWPLEEGSslRYGDLTVtnlSVENKEHY----------KKTTLEI--------HNTETD-ESR--QVT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 536 QVRM--WPiENKVPLSTTGLID------------VIKMARSWRKrapdRPETKPTIVMSHNGVSRVGVYIGANICIDQMD 601
Cdd:cd14543  164 HFQFtsWP-DFGVPSSAAALLDflgevrqqqalaVKAMGDRWKG----HPPGPPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 212645549 602 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
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: 73.04 E-value: 7.13e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 372 TLRIGDCAGGHRLENRGKNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIY 451
Cdd:cd14604   43 TEKIYPTATGEKEENVKKNRYKDILPFDHSRVKL-TLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIW 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 452 DHACHTVV------NLSNQGSQRHYPsfIHNKGKANYGPFIVEIMNYHqypAMTSHMVkvmkRTFMIsdimatgaqnqQI 525
Cdd:cd14604  122 EYNVAIIVmacrefEMGRKKCERYWP--LYGEEPMTFGPFRISCEAEQ---ARTDYFI----RTLLL-----------EF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 526 DAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM---- 600
Cdd:cd14604  182 QNETRRLYQFHYVNWP-DHDVPSSFDSILDMISLMRKYQEH-----EDVPICIHCSAGCGRTGA-----ICaIDYTwnll 250

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 212645549 601 ---DIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
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: 1.49e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsqrhypsfIHNKGKanygpfiveiMNYHQYP 496
Cdd:cd14616   27 YINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQ----------CFEKGR----------IRCHQYW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 497 AMTSHMVKVMkrtfmiSDIMATG-AQNQQIDAEVRICCV------IQVRM-----WPiENKVPLSTTGLIDVIKMARSWR 564
Cdd:cd14616   87 PEDNKPVTVF------GDIVITKlMEDVQIDWTIRDLKIerhgdyMMVRQcnftsWP-EHGVPESSAPLIHFVKLVRASR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 565 KRapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDiDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 633
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: 1.67e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 383 RLENRGKNRDVMVVPPDHAR------------------PYLQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVD 444
Cdd:PHA02746  48 KKENLKKNRFHDIPCWDHSRvvinaheslkmfdvgdsdGKKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 445 SFWTLIYDHACHTVVNLS--NQGSQRHYPSFIHNKG-KANYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISDIMATGAq 521
Cdd:PHA02746 128 DFFKLISEHESQVIVSLTdiDDDDEKCFELWTKEEDsELAFGRFVAKILDIIEELSFT-------KTRLMITDKISDTS- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 522 nqqidaevRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR----APDRPETK-PTIVMSHNGVSRVGVYIGANIC 596
Cdd:PHA02746 200 --------REIHHFWFPDWP-DNGIPTGMAEFLELINKVNEEQAElikqADNDPQTLgPIVVHCSAGIGRAGTFCAIDNA 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 212645549 597 IDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVM 636
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: 2.71e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINA----VEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQRHYPSFihnkgkaNYGPFiveiMNY 492
Cdd:cd14540    1 YINAshitATVGGKQRF--YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCF-------RYWPT----LGG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 493 HqYPAMTSHMVKVMKRTFMISDIMATGA---QNQQIDAEvRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKR--- 566
Cdd:cd14540   68 E-HDALTFGEYKVSTKFSVSSGCYTTTGlrvKHTLSGQS-RTVWHLQYTDWP-DHGCPEDVSGFLDFLEEINSVRRHtnq 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645549 567 --APDRPETkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
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: 65.93 E-value: 3.72e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEV-DGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS------NQGSQRHYPsfihNKGKANYGPFIVEI 489
Cdd:cd14546    1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTrlqengVKQCARYWP----EEGSEVYHIYEVHL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 490 MNYHQYPAmtSHMVkvmkRTFMISDImatgaQNQqidaEVRICCVIQVRMWPIENkVPLSTTGLIDV-IKMARSWRKRap 568
Cdd:cd14546   77 VSEHIWCD--DYLV----RSFYLKNL-----QTS----ETRTVTQFHFLSWPDEG-IPASAKPLLEFrRKVNKSYRGR-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212645549 569 drpeTKPTIVMSHNGVSRVGVYIGANICIDQMDID-HEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
Cdd:cd14546  139 ----SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 67.30 E-value: 5.37e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 107 RVILPRIDGDENSHYINASYVNSWLRDKAYVVTQAVRTKPMNaEFWRMVWELGSNCIVMLTKVFDfmRVMCLQYWPL--- 183
Cdd:PHA02740  64 RLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACD-KFLQALSDNKVQIIVLISRHAD--KKCFNQFWSLkeg 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 184 TKFQFREIEVETTEVKTYSHFVIRTFKLTRTTPESietRIVKHFHFTEWELDSFPY-ISAFIELRRRVRQF---MEKNPV 259
Cdd:PHA02740 141 CVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA---QKISHFQYTAWPADGFSHdPDAFIDFFCNIDDLcadLEKHKA 217

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 260 E---APMVVHCSNGAGRSGAFLALDANLELMKKTGQLDFFEYAKTLVNSRPHLIDSVEQYMFIYEVL 323
Cdd:PHA02740 218 DgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284

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: 6.72e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 390 NRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRK-AEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--QGS 466
Cdd:cd14547    1 NRYKTILPNEHSRVCL-PSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNltEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 467 QR--HYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTShmvkvmkRTFMIsdimatgaqnqQIDAEVRICCVIQVRMWPiEN 544
Cdd:cd14547   80 EKcaQYWPEEENE---TYGDFEVTVQSVKETDGYTV-------RKLTL-----------KYGGEKRYLKHYWYTSWP-DH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 545 KVPLSTTGLIDVIKMARSWRKRAPDRPetkPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLID 624
Cdd:cd14547  138 KTPEAAQPLLSLVQEVEEARQTEPHRG---PIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQ 214


                 ....*....
gi 212645549 625 MKDEYKYLY 633
Cdd:cd14547  215 TAEQYEFVH 223

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 66.95 E-value: 7.13e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 383 RLENRGKNRDVMVVPPDHARPYLQTLHGESKdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS 462
Cdd:PHA02742  49 ELKNMKKCRYPDAPCFDRNRVILKIEDGGDD---FINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMIT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 ---NQGSQRHYPSFI-HNKGKANYGPFIV---EIMNYHQYPAMTSHMVKVmkRTFMISDIMATGAQNqqidaevriccvi 535
Cdd:PHA02742 126 kimEDGKEACYPYWMpHERGKATHGEFKIktkKIKSFRNYAVTNLCLTDT--NTGASLDIKHFAYED------------- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 536 qvrmWPiENKVPLSTTGLIDVIKMARSWRKRA------PDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVF 609
Cdd:PHA02742 191 ----WP-HGGLPRDPNKFLDFVLAVREADLKAdvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265

                        250       260       270
                 ....*....|....*....|....*....|
gi 212645549 610 HAVKMMRINRPQLIDMKDEYKYLYDVMLHW 639
Cdd:PHA02742 266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295

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: 66.06 E-value: 8.56e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 381 GHRLENRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVD----GFTRKAE-FIVTEWPKQSTVDSFWTLIYDHAC 455
Cdd:cd14606   13 GQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKtYIASQGCLEATVNDFWQMAWQENS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 456 HTVVNLSNQ---GSQRHYPSFIHNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKrtfmISDIMATGAqnqqidaeVRIC 532
Cdd:cd14606   93 RVIVMTTREvekGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD---TTEYKLRTLQ----VSPLDNGEL--------IREI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 533 CVIQVRMWPiENKVPLSTTGlidVIKMARSWRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 609
Cdd:cd14606  158 WHYQYLSWP-DHGVPSEPGG---VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStkgLDCDIDIQ 233

                        250       260
                 ....*....|....*....|....
gi 212645549 610 HAVKMMRINRPQLIDMKDEYKYLY 633
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: 2.27e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 389 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNqgsq 467
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITN---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 468 rhypsfihnkgkanygpfiVEIMN-----YHQYPAMTSHMVKVMKRTFMISDIMATGAQNQQIDAEVRICCVIQVRMWPi 542
Cdd:cd14613  104 -------------------IEEMNekcteYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWP- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 543 ENKVPLSTTGLIDVIKMARSWRKRAPdrPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQL 622
Cdd:cd14613  164 DQKTPDNAPPLLQLVQEVEEARQQAE--PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241

                        250
                 ....*....|....
gi 212645549 623 IDMKDEYKYLYDVM 636
Cdd:cd14613  242 IQTCEQYQFVHHVL 255

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 62.63 E-value: 7.29e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 389 KNRDVMVVPPDHARPYLQTLHGESKDYTYINAVEVDGFTRKAE-FIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQGSQ 467
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 468 RHYPSFIHNKGKANYGPFIVEIMNYHQYPAMTShmvkvmkRTFMISDimatGAQNQQIDAevriccvIQVRMWPiENKVP 547
Cdd:cd14611   82 NEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTI-------RNLTLKQ----GSQSRSVKH-------YWYTSWP-DHKTP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 548 LSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKD 627
Cdd:cd14611  143 DSAQPLLQLMLDVEEDRLASPGR---GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSE 219


                 ....*.
gi 212645549 628 EYKYLY 633
Cdd:cd14611  220 QYEFVH 225

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 63.79 E-value: 8.37e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARpylQTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ- 464
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSR---VILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKk 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 465 --GSQRHYPSFIH-NKGKANYGPFIVEIMNYHQYPamtsHMVkvmKRTFMISDimATGAQNQQIDaevriccvIQVRMWP 541
Cdd:PHA02738 126 enGREKCFPYWSDvEQGSIRFGKFKITTTQVETHP----HYV---KSTLLLTD--GTSATQTVTH--------FNFTAWP 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 542 iENKVPLSTTGLIDVIKMARSWRKR--------APDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVK 613
Cdd:PHA02738 189 -DHDVPKNTSEFLNFVLEVRQCQKElaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVS 267

                        250       260
                 ....*....|....*....|...
gi 212645549 614 MMRINRPQLIDMKDEYKYLYDVM 636
Cdd:PHA02738 268 SIRNQRYYSLFIPFQYFFCYRAV 290

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: 1.31e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKA-EFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQG------SQRHYPSfihNKGKA-NYGPFIVE 488
Cdd:cd14539    1 YINASLIEDLTPYCpRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQenekqkVHRYWPT---ERGQAlVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 489 IMNYHQYPAMTSHMVKVMKRTfmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 568
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKD----------------TRLSRSVVHLQFTTWP-ELGLPDSPNPLLRFIEEVHSHYLQ-- 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212645549 569 DRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEV-DVFHAVKMMRINRPQLIDMKDEYKYLYD 634
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: 1.55e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSnqgsqrhypSFIHNKGKANYGPFIVEIMNYHQ 494
Cdd:cd17658    1 YINAslVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLT---------RLVDNYSTAKCADYFPAEENESR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 495 YPAMTSHMVKVMKRTfmISDIMATGAQNQQIDAEVRICCV--IQVRMWPiENKVPLSTTGLIDVIKmaRSWrkRAPdrPE 572
Cdd:cd17658   72 EFGRISVTNKKLKHS--QHSITLRVLEVQYIESEEPPLSVlhIQYPEWP-DHGVPKDTRSVRELLK--RLY--GIP--PS 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212645549 573 TKPTIVMSHNGVSRVGVYIGANICIDQ-MDIDHE-VDVFHAVKMMRINRPQLIDMKDEYKYLY 633
Cdd:cd17658  143 AGPIVVHCSAGIGRTGAYCTIHNTIRRiLEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.

Pssm-ID: 350392 [Multi-domain] Cd Length: 251 Bit Score: 60.55 E-value: 4.96e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 386 NRGKNRDVMVVPPDHARPYLQTLHGESKDYTYINA----VEVDGFTRKAE---FIVTEWPKQSTVDSFWTLIYDHACHTV 458
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINAnyirNENEGPTTDENaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 459 VNLS---NQGSQ---RHYPSFIHNKgkaNYGPFIVEIMNYHQYPAMTshmvkvmKRTFMISdimaTGAQNqqidAEVRIC 532
Cdd:cd14544   81 VMTTkevERGKNkcvRYWPDEGMQK---QYGPYRVQNVSEHDTTDYT-------LRELQVS----KLDQG----DPIREI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 533 CVIQVRMWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMD---IDHEVDVF 609
Cdd:cd14544  143 WHYQYLSWP-DHGVPSDPGGVLNFLEDV---NQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKrkgLDCDIDIQ 218

                        250       260       270
                 ....*....|....*....|....*....|...
gi 212645549 610 HAVKMMRINRPQLIDMKDEYKYLYDVMLHWYMT 642
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: 1.52e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQtlhgESKDY---TYINaVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNL 461
Cdd:cd14600   39 QNMDKNRYKDVLPYDATRVVLQ----GNEDYinaSYVN-MEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 462 SNqgsqrhypsfIHNKGKA---NYGPFIVEIMNYHQYpAMTSHM----VKVMKRTFMISDImATGAQnqqidaevRICCV 534
Cdd:cd14600  114 TT----------LTERGRTkchQYWPDPPDVMEYGGF-RVQCHSedctIAYVFREMLLTNT-QTGEE--------RTVTH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 535 IQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKM 614
Cdd:cd14600  174 LQYVAWP-DHGVPDDSSDFLEFVNYVRSKRV------ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK 246

                        250       260
                 ....*....|....*....|....*.
gi 212645549 615 MRINRPQLIDMKDEYKYLYDVMLHWY 640
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: 58.31 E-value: 2.47e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 389 KNRDVMVVPPDHARPYLqTLHGESKDYTYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV------NLS 462
Cdd:cd14602    1 KNRYKDILPYDHSRVEL-SLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVmacmefEMG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 NQGSQRHYPSFihNKGKANYGPFIVEIMNYHQypaMTSHMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPi 542
Cdd:cd14602   80 KKKCERYWAEP--GEMQLEFGPFSVTCEAEKR---KSDYIIRTLKVKF---------------NSETRTIYQFHYKNWP- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 543 ENKVPLSTTGLIDVIKMARSWRKRapdrpETKPTIVMSHNGVSRVGVyiganIC-IDQM-------DIDHEVDVFHAVKM 614
Cdd:cd14602  139 DHDVPSSIDPILELIWDVRCYQED-----DSVPICIHCSAGCGRTGV-----ICaIDYTwmllkdgIIPENFSVFSLIQE 208

                        250       260
                 ....*....|....*....|....*.
gi 212645549 615 MRINRPQLIDMKDEYKYLYDVMLHWY 640
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: 1.19e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVV------NLSNQGSQRHYPSfihNKGKA-NYGPFIVEi 489
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVmacrefEMGKKKCERYWPE---EGEEQlQFGPFKIS- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 490 mnYHQYPAMTS-HMVKVMKRTFmisdimatgaqnqqiDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKRap 568
Cdd:cd14542   77 --LEKEKRVGPdFLIRTLKVTF---------------QKESRTVYQFHYTAWP-DHGVPSSVDPILDLVRLVRDYQGS-- 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212645549 569 drpETKPTIVMSHNGVSRVGVyiganIC-ID--------QMdIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLY 633
Cdd:cd14542  137 ---EDVPICVHCSAGCGRTGT-----ICaIDyvwnllktGK-IPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 56.57 E-value: 1.65e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPylqTLHGESKDYTYINAVEVDGFTRKaeFIVTEWPKQSTVDSFWTLIYDHACHTVVNLS-- 462
Cdd:cd14608   24 KNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRS--YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNrv 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 -NQGS---QRHYPsfihnkgKANYGPFIVEIMNYHqypamTSHMVKVMKRTFMISDIMATGAQNQqidaEVRICCVIQVR 538
Cdd:cd14608   99 mEKGSlkcAQYWP-------QKEEKEMIFEDTNLK-----LTLISEDIKSYYTVRQLELENLTTQ----ETREILHFHYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 539 MWPiENKVPLSTTGLIDVIKMArswRKRAPDRPETKPTIVMSHNGVSRVGVYIGANICIDQMDIDHE---VDVFHAVKMM 615
Cdd:cd14608  163 TWP-DFGVPESPASFLNFLFKV---RESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEM 238

                        250
                 ....*....|....*...
gi 212645549 616 RINRPQLIDMKDEYKYLY 633
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: 54.45 E-value: 4.06e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGeskdytYINAVEVDGFTRKAEF--IVTEWPKQSTVDSFWTLIYDHACHTVVNLS 462
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLGDEGG------YINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 463 NQ------GSQRHYPsfihnkgkanygpfiveimnyhqypamtshmvKVMKRTFMISD-IMATGAQNQQIDA-------- 527
Cdd:cd14597   76 QEveggkiKCQRYWP--------------------------------EILGKTTMVDNrLQLTLVRMQQLKNfvirvlel 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 528 ------EVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKrapdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMD 601
Cdd:cd14597  124 ediqtrEVRHITHLNFTAWP-DHDTPSQPEQLLTFISYMRHIHK-------SGPIITHCSAGIGRSGTLICIDVVLGLIS 195

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 212645549 602 IDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVMLH 638
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: 2.35e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 417 YINA--VEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNQ------GSQRHYPSFIHNKGK-ANYGPFIV 487
Cdd:cd14596    1 YINAsyITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREvergkvKCHRYWPETLQEPMElENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 488 eimnyhQYPAMTSHMVKVMKRTfmisdimatgaqnQQIDAEVRICCVIQVRMWPiENKVPLSTTGLIDVIKMARSWRKra 567
Cdd:cd14596   81 ------NYQALQYFIIRIIKLV-------------EKETGENRLIKHLQFTTWP-DHGTPQSSDQLVKFICYMRKVHN-- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 568 pdrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDHEVDVFHAVKMMRINRPQLIDMKDEYKYLYDVML 637
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: 1.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 385 ENRGKNRDVMVVPPDHARPYLQTLHGEskdytYINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSNq 464
Cdd:cd14607   23 ENRNRNRYRDVSPYDHSRVKLQNTEND-----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNR- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 465 gsqrhypsfIHNKGK---ANYGPFIVEIMNYHQYPAMTSHMVKVMKRTFMISDIMatgaQNQQIDA-EVRICCVIQVRMW 540
Cdd:cd14607   97 ---------IVEKDSvkcAQYWPTDEEEVLSFKETGFSVKLLSEDVKSYYTVHLL----QLENINSgETRTISHFHYTTW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 541 PiENKVPLSTTGLIDVIKMARSWRKRAPDRpetKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 618
Cdd:cd14607  164 P-DFGVPESPASFLNFLFKVRESGSLSPEH---GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKY 239

                        250
                 ....*....|....*
gi 212645549 619 RPQLIDMKDEYKYLY 633
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: 3.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 387 RGKNRDVMVVPPDHARPYLQtlhGESKDYtyINAVEVDGFTRKAEFIVTEWPKQSTVDSFWTLIYDHACHTVVNLSN--- 463
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK---QGDNDY--INASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKlme 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 464 QGSQRHYPSFIHNKGKANYGP---FIVEIMNYHQYPAMTshmvkvmKRTFMISDImATGaqnqqidaEVRICCVIQVRMW 540
Cdd:cd14545   76 KGQIKCAQYWPQGEGNAMIFEdtgLKVTLLSEEDKSYYT-------VRTLELENL-KTQ--------ETREVLHFHYTTW 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212645549 541 PiENKVPLSTTGLIDVIKMARSWRKRAPDrpeTKPTIVMSHNGVSRVGVYIGANICIDQMDIDH--EVDVFHAVKMMRIN 618
Cdd:cd14545  140 P-DFGVPESPAAFLNFLQKVRESGSLSSD---VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKY 215

                        250
                 ....*....|....*
gi 212645549 619 RPQLIDMKDEYKYLY 633
Cdd:cd14545  216 RMGLIQTPDQLRFSY 230