NCBI Conserved Domain Search

Conserved domains on [gi|2075913722|gb|KAG8451101|]

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hypothetical protein GDO86_003389 [Hymenochirus boettgeri]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PTP_DSP_cys super family

cl28904

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

4-177

3.16e-76

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

The actual alignment was detected with superfamily member cd14548:

Pssm-ID: 475123 [Multi-domain] Cd Length: 222 Bit Score: 229.16 E-value: 3.16e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   4 RYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVL 83
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  84 CDQYWPSET--AAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVREE 161
Cdd:cd14548    81 CDHYWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170
                  ....*....|....*.
gi 2075913722 162 IQitKGPGPTVLHCRN 177
Cdd:cd14548   157 IK--QEKGPTIVHCSA 170

Name

Accession

Description

Interval

E-value

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

4-177

3.16e-76

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: 229.16 E-value: 3.16e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   4 RYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVL 83
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  84 CDQYWPSET--AAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVREE 161
Cdd:cd14548    81 CDHYWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170
                  ....*....|....*.
gi 2075913722 162 IQitKGPGPTVLHCRN 177
Cdd:cd14548   157 IK--QEKGPTIVHCSA 170

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-177

2.69e-73

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 222.92 E-value: 2.69e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722    1 MKNRYSYILPYDHSRVKLTLIDGkQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:smart00194  29 DKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   81 KVLCDQYWPSETAA---YGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAEL 157
Cdd:smart00194 108 REKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSETRTVTHYHYTNWPDHGVPESPESILDLIRA 185

                          170       180
                   ....*....|....*....|
gi 2075913722  158 VREEIQITKgpGPTVLHCRN 177
Cdd:smart00194 186 VRKSQSTST--GPIVVHCSA 203

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-177

2.71e-70

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 214.41 E-value: 2.71e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   1 MKNRYSYILPYDHSRVKLTliDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYWPS---ETAAYGPFTVQKVSEV-ICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:pfam00102  81 REKCAQYWPEeegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGG--SEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180
                  ....*....|....*....|.
gi 2075913722 157 LVREEiQITKGPGPTVLHCRN 177
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSA 178

PHA02738

hypothetical protein; Provisional

3-175

2.39e-31

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 116.95 E-value: 2.39e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVklTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:PHA02738   53 NRYLDAVCFDHSRV--ILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGRE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWPS---ETAAYGPFTVQKVSevickewTIRHL----TINRLKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFA 155
Cdd:PHA02738  131 KCFPYWSDveqGSIRFGKFKITTTQ-------VETHPhyvkSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2075913722 156 --------ELVREEIQI---TKGPGPTVLHC 175
Cdd:PHA02738  204 levrqcqkELAQESLQIghnRLQPPPIVVHC 234

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2-176

6.73e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 112.11 E-value: 6.73e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKltlidgkQDSGYINANYIQGfSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:COG5599    45 LNRFRDIQPYKETALR-------ANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 --VLCDQYWPSEtAAYGPFTVQkvSEVICKEWTIRHLTIN----RLKDVDSPVRHISQLHYTAWPDRGIPhNPSSLITFA 155
Cdd:COG5599   117 pkVKMPVYFRQD-GEYGKYEVS--SELTESIQLRDGIEARtyvlTIKGTGQKKIEIPVLHVKNWPDHGAI-SAEALKNLA 192

                         170       180
                  ....*....|....*....|..
gi 2075913722 156 ELVREEIQITKGP-GPTVLHCR 176
Cdd:COG5599   193 DLIDKKEKIKDPDkLLPVVHCR 214

Name

Accession

Description

Interval

E-value

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

4-177

3.16e-76

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 229.16 E-value: 3.16e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   4 RYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVL 83
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  84 CDQYWPSET--AAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVREE 161
Cdd:cd14548    81 CDHYWPFDQdpVYYGDITVTMLSESVLPDWTIREFKLERGDE----VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                         170
                  ....*....|....*.
gi 2075913722 162 IQitKGPGPTVLHCRN 177
Cdd:cd14548   157 IK--QEKGPTIVHCSA 170

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1-177

2.69e-73

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 222.92 E-value: 2.69e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722    1 MKNRYSYILPYDHSRVKLTLIDGkQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:smart00194  29 DKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   81 KVLCDQYWPSETAA---YGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAEL 157
Cdd:smart00194 108 REKCAQYWPDEEGEpltYGDITVTLKSVEKVDDYTIRTLEVTNTG--CSETRTVTHYHYTNWPDHGVPESPESILDLIRA 185

                          170       180
                   ....*....|....*....|
gi 2075913722  158 VREEIQITKgpGPTVLHCRN 177
Cdd:smart00194 186 VRKSQSTST--GPIVVHCSA 203

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

3-175

1.69e-72

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: 220.20 E-value: 1.69e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWPSETA--AYGPFTVQKVSEVICKEWTIRHLTINRlkDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14618    81 LCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWH--EDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170
                  ....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC 175
Cdd:cd14618   159 HVQATKGKGPTLVHC 173

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1-177

2.71e-70

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 214.41 E-value: 2.71e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   1 MKNRYSYILPYDHSRVKLTliDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYWPS---ETAAYGPFTVQKVSEV-ICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:pfam00102  81 REKCAQYWPEeegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGG--SEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180
                  ....*....|....*....|.
gi 2075913722 157 LVREEiQITKGPGPTVLHCRN 177
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSA 178

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

3-175

1.39e-67

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: 207.46 E-value: 1.39e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWP--SETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSPvRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14617    81 KCDHYWPadQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAP-RLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170
                  ....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC 175
Cdd:cd14617   160 YINRTPGSGPTVVHC 174

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

3-194

5.37e-66

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

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 203.58 E-value: 5.37e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWP--SETAAYGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14619    81 KCEHYWPldYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14619   159 WLDQTMSGGPTVVHCsagvgRTGTLIALDVLLQQLQSEG 197

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

2-190

9.25e-64

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: 198.00 E-value: 9.25e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14553     6 KNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14553    86 VKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALHKNG--SSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2075913722 161 EIQitKGPGPTVLHC-----RNNIYLCIAVYLKKV 190
Cdd:cd14553   164 CNP--PDAGPIVVHCsagvgRTGCFIVIDSMLERI 196

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

3-175

7.60e-62

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: 192.72 E-value: 7.60e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTlIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDS-PVRHisqLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14615    80 KCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESrTVRH---FHFTSWPDHGVPETTDLLINFRHLVRE 156

                         170
                  ....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC 175
Cdd:cd14615   157 YMKQNPPNSPILVHC 171

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

29-177

1.49e-60

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: 188.65 E-value: 1.49e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE---TAAYGPFTVQKVSE 105
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEggkPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075913722 106 VICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQitKGPGPTVLHCRN 177
Cdd:cd00047    81 EELSDYTIRTLELSPKG--CSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSA 148

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

2-175

3.15e-58

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: 184.88 E-value: 3.15e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14543    32 KNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE---TAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELV 158
Cdd:cd14543   112 VKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDES--RQVTHFQFTSWPDFGVPSSAAALLDFLGEV 189

                         170       180
                  ....*....|....*....|....*....
gi 2075913722 159 REEIQI------------TKGPgPTVLHC 175
Cdd:cd14543   190 RQQQALavkamgdrwkghPPGP-PIVVHC 217

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

3-175

1.83e-57

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: 181.44 E-value: 1.83e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANE-YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEhGK 81
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINRlkdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14547    80 EKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKY----GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                         170
                  ....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC 175
Cdd:cd14547   156 ARQTEPHRGPIVVHC 170

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

2-175

2.58e-57

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: 182.33 E-value: 2.58e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14603    33 KNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPS--ETAAYGPFTVQKVSEVICKEWTI-RHLTINrLKDVDspvRHISQLHYTAWPDRGIPHNPSSLITFAELV 158
Cdd:cd14603   113 KKCERYWAQeqEPLQTGPFTITLVKEKRLNEEVIlRTLKVT-FQKES---RSVSHFQYMAWPDHGIPDSPDCMLAMIELA 188

                         170
                  ....*....|....*..
gi 2075913722 159 REEIQitKGPGPTVLHC 175
Cdd:cd14603   189 RRLQG--SGPEPLCVHC 203

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

2-175

5.22e-57

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: 181.24 E-value: 5.22e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14614    15 KNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWP--SETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIP--HNPSSLITFAEL 157
Cdd:cd14614    95 VKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE----VQDVMHFNYTAWPDHGVPtaNAAESILQFVQM 170

                         170
                  ....*....|....*...
gi 2075913722 158 VREeiQITKGPGPTVLHC 175
Cdd:cd14614   171 VRQ--QAVKSKGPMIIHC 186

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

29-195

8.95e-54

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: 171.38 E-value: 8.95e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE-TAAYGPFTVQKVSEVI 107
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 108 CKEWTIRHLTINRLK----DVDSPVRHISQLHYTAWPDRGIPHNPSSLITFaelVREEIQIT-KGPGPTVLHC-----RN 177
Cdd:cd14549    81 LATYTVRTFSLKNLKlkkvKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANpPGAGPIVVHCsagvgRT 157

                         170
                  ....*....|....*...
gi 2075913722 178 NIYLCIAVYLKKVYRRGK 195
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGT 175

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

2-190

1.12e-51

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: 168.29 E-value: 1.12e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14626    44 KNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINrlKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFaeLVRE 160
Cdd:cd14626   124 VKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALY--KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF--LRRV 199

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKV 190
Cdd:cd14626   200 KACNPPDAGPMVVHCsagvgRTGCFIVIDAMLERM 234

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

2-194

1.49e-50

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: 165.59 E-value: 1.49e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGK--QDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEH 79
Cdd:cd17667    30 KNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  80 GKVLCDQYWPSETA-AYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSP---------VRHISQLHYTAWPDRGIPHNPS 149
Cdd:cd17667   110 GRRKCDQYWPTENSeEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQkgnpkgrqnERTVIQYHYTQWPDMGVPEYAL 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2075913722 150 SLITFAElvREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd17667   190 PVLTFVR--RSSAARTPEMGPVLVHCsagvgRTGTYIVIDSMLQQIKDKS 237

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

2-194

4.28e-50

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: 163.40 E-value: 4.28e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQD-SGYINANYIQ-------GFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVML 73
Cdd:cd14544     4 KNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  74 TVCEEHGKVLCDQYWPSE--TAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSPvRHISQLHYTAWPDRGIPHNPSSL 151
Cdd:cd14544    84 TKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDHGVPSDPGGV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2075913722 152 ITFAELVREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14544   163 LNFLEDVNQRQESLPHAGPIVVHCsagigRTGTFIVIDMLLDQIKRKG 210

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

2-179

7.45e-50

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: 162.70 E-value: 7.45e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGK-QDSGYINANYIQGFSGA-NEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEh 79
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAGSQeEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  80 GKVLCDQYWPSETAAYGPFT--VQKVSEviCKEWTIRHLTINrlkdVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAEL 157
Cdd:cd14612    97 KKEKCVHYWPEKEGTYGRFEirVQDMKE--CDGYTIRDLTIQ----LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAE 170

                         170       180
                  ....*....|....*....|..
gi 2075913722 158 VREEIQITKGPGPTVLHCRNNI 179
Cdd:cd14612   171 VEESRQTAASPGPIVVHCSAGI 192

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

2-179

8.08e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 159.48 E-value: 8.08e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDsgYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDND--YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAA-----YGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:cd14545    79 IKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180
                  ....*....|....*....|...
gi 2075913722 157 LVREEIQITKGPGPTVLHCRNNI 179
Cdd:cd14545   157 KVRESGSLSSDVGPPVVHCSAGI 179

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

3-175

1.14e-48

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: 158.92 E-value: 1.14e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWPSET---AAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVR 159
Cdd:cd14616    81 RCHQYWPEDNkpvTVFGDIVITKLMEDVQIDWTIRDLKIERHGD----YMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                         170
                  ....*....|....*.
gi 2075913722 160 EeiQITKGPGPTVLHC 175
Cdd:cd14616   157 A--SRAHDNTPMIVHC 170

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

2-190

1.21e-48

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: 159.61 E-value: 1.21e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14554     9 KNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREMGR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAA-YGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14554    89 EKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDAR--DGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKV 190
Cdd:cd14554   167 TKEQFGQEGPITVHCsagvgRTGVFITLSIVLERM 201

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

29-175

3.03e-48

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: 157.41 E-value: 3.03e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQ-GFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAA--YGPFTV--QKV 103
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgeYGDLTVelVSE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075913722 104 SEVICKEWTIRHLTINRlkdVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKGPGPTVLHC 175
Cdd:cd18533    81 EENDDGGFIVREFELSK---EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHC 149

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

2-175

6.32e-48

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: 159.33 E-value: 6.32e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14604    60 KNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWP---SETAAYGPFTVQKVSEVICKEWTIRHLTInrlkDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELV 158
Cdd:cd14604   140 KKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLL----EFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                         170
                  ....*....|....*..
gi 2075913722 159 REEIQITKgpGPTVLHC 175
Cdd:cd14604   216 RKYQEHED--VPICIHC 230

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

2-190

2.02e-47

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: 157.56 E-value: 2.02e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14625    50 KNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINrlKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRe 160
Cdd:cd14625   130 IKCDQYWPSRgTETYGMIQVTLLDTIELATFCVRTFSLH--KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK- 206

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075913722 161 eiqiTKGP---GPTVLHC-----RNNIYLCIAVYLKKV 190
Cdd:cd14625   207 ----TCNPpdaGPIVVHCsagvgRTGCFIVIDAMLERI 240

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1-194

3.22e-47

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: 156.74 E-value: 3.22e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   1 MKNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:cd14633    42 MKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYWPSETAAYGPFTVQKVSEVICKEWTIRHLTINrlKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14633   122 RVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE--KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS 199

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075913722 161 eiQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14633   200 --KSPPNAGPLVVHCsagagRTGCFIVIDIMLDMAEREG 236

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

2-190

5.29e-47

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: 156.82 E-value: 5.29e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14624    50 KNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRhlTINRLKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVRe 160
Cdd:cd14624   130 VKCDQYWPSRgTETYGLIQVTLLDTVELATYCVR--TFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK- 206

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075913722 161 eiqiTKGP---GPTVLHC-----RNNIYLCIAVYLKKV 190
Cdd:cd14624   207 ----TCNPpdaGPMVVHCsagvgRTGCFIVIDAMLERI 240

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

5-175

2.27e-45

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: 150.86 E-value: 2.27e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   5 YSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLC 84
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  85 DQYWPSETA-AYGPFTVQKVSEVICKEWTIRHLTIN-RLKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVReei 162
Cdd:cd14620    81 YQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQpQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK--- 157

                         170
                  ....*....|....*.
gi 2075913722 163 qiTKGP---GPTVLHC 175
Cdd:cd14620   158 --SVNPvhaGPIVVHC 171

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

2-175

2.85e-45

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: 150.95 E-value: 2.85e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14630     6 KNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEVGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDspVRHISQLHYTAWPDRGIPHNPSSLITFAelvrEE 161
Cdd:cd14630    86 VKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHE--IREIRQFHFTSWPDHGVPCYATGLLGFV----RQ 159

                         170
                  ....*....|....*.
gi 2075913722 162 IQITKGP--GPTVLHC 175
Cdd:cd14630   160 VKFLNPPdaGPIVVHC 175

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

2-175

3.64e-45

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: 152.10 E-value: 3.64e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14621    55 KNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETA-AYGPFTVQKVSEVICKEWTIRHLTINRLKDVDS--PVRHISQLHYTAWPDRGIPHNPSSLITFAELV 158
Cdd:cd14621   135 CKCAQYWPDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNkkPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKV 214

                         170       180
                  ....*....|....*....|
gi 2075913722 159 ReeiqiTKGP---GPTVLHC 175
Cdd:cd14621   215 K-----NCNPqyaGAIVVHC 229

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

2-175

4.35e-45

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: 149.99 E-value: 4.35e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWP---SETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDvdspVRHISQLHYTAWPDRGIphnPSSLITFAELV 158
Cdd:cd14602    81 KKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSE----TRTIYQFHYKNWPDHDV---PSSIDPILELI 153

                         170
                  ....*....|....*...
gi 2075913722 159 REEIQITKGPG-PTVLHC 175
Cdd:cd14602   154 WDVRCYQEDDSvPICIHC 171

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

2-201

2.64e-43

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: 146.32 E-value: 2.64e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTliDG---KQDSGYINANYI--------QGFSGANEYIATQAPMPATFDDFWRMVWEKEVRII 70
Cdd:cd14605     5 KNRYKNILPFDHTRVVLH--DGdpnEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  71 VMLTVCEEHGKVLCDQYWPSETA--AYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSPvRHISQLHYTAWPDRGIPHNP 148
Cdd:cd14605    83 VMTTKEVERGKSKCVKYWPDEYAlkEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTE-RTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075913722 149 SSLITFAELVREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG------KPQSITM 201
Cdd:cd14605   162 GGVLDFLEEVHHKQESIMDAGPVVVHCsagigRTGTFIVIDILIDIIREKGvdcdidVPKTIQM 225

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

2-187

4.84e-43

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: 144.97 E-value: 4.84e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLtlidgKQDSGYINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEH 79
Cdd:cd14597     6 KNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  80 GKVLCDQYWPSEtaaygPFTVQKVSEVI---------CKEWTIRHLTinrLKDVDS-PVRHISQLHYTAWPDRGIPHNPS 149
Cdd:cd14597    81 GKIKCQRYWPEI-----LGKTTMVDNRLqltlvrmqqLKNFVIRVLE---LEDIQTrEVRHITHLNFTAWPDHDTPSQPE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2075913722 150 SLITFAELVReeiQITKGpGPTVLHC-----RNNIYLCIAVYL 187
Cdd:cd14597   153 QLLTFISYMR---HIHKS-GPIITHCsagigRSGTLICIDVVL 191

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

2-179

1.47e-42

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: 144.64 E-value: 1.47e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGK-QDSGYINANYIQG-FSGANE----YIATQAPMPATFDDFWRMVWEKEVRIIVMLTV 75
Cdd:cd14606    21 KNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGPDEnaktYIASQGCLEATVNDFWQMAWQENSRVIVMTTR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  76 CEEHGKVLCDQYWPS--ETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSPvRHISQLHYTAWPDRGIPHNPSSLIT 153
Cdd:cd14606   101 EVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELI-REIWHYQYLSWPDHGVPSEPGGVLS 179

                         170       180
                  ....*....|....*....|....*.
gi 2075913722 154 FAELVREEIQITKGPGPTVLHCRNNI 179
Cdd:cd14606   180 FLDQINQRQESLPHAGPIIVHCSAGI 205

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

29-195

1.51e-42

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: 142.66 E-value: 1.51e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPS---ETAAYGPFTVQKVSE 105
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeeGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 106 VICKEWTIRHLTINRLKDVDSPvRHISQLHYTAWPDRGIPHNPSSLITfaelVREEIQITKG--PGPTVLHC-----RNN 178
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLK----LRRRVNAFNNffSGPIVVHCsagvgRTG 155

                         170
                  ....*....|....*..
gi 2075913722 179 IYLCIAVYLKKVYRRGK 195
Cdd:cd14557   156 TYIGIDAMLEGLEAEGR 172

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

2-199

3.01e-42

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: 144.01 E-value: 3.01e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTlidgKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14608    28 RNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAAYGPF-----TVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:cd14608   104 LKCAQYWPQKEEKEMIFedtnlKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFGVPESPASFLNFLF 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2075913722 157 LVREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRGKPQSI 199
Cdd:cd14608   182 KVRESGSLSPEHGPVVVHCsagigRSGTFCLADTCLLLMDKRKDPSSV 229

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

2-210

6.95e-42

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: 143.72 E-value: 6.95e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14627    56 KNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAA-YGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14627   136 EKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRGKP---QSITMDHMKMPTVL 210
Cdd:cd14627   214 TKEQFGQDGPISVHCsagvgRTGVFITLSIVLERMRYEGVVdifQTVKMLRTQRPAMV 271

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

2-210

8.49e-42

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: 143.33 E-value: 8.49e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14628    55 KNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAA-YGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14628   135 EKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 212

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRGKP---QSITMDHMKMPTVL 210
Cdd:cd14628   213 TKEQFGQDGPISVHCsagvgRTGVFITLSIVLERMRYEGVVdifQTVKMLRTQRPAMV 270

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

2-205

1.09e-41

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: 142.89 E-value: 1.09e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGAN-EYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:cd14610    47 KNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYWPSE-TAAYGPFTVQKVSEVI-CKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELV 158
Cdd:cd14610   127 VKQCYHYWPDEgSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNET--RTVTQFHFLSWNDQGVPASTRSLLDFRRKV 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2075913722 159 ReeiQITKGPG-PTVLHC-----RNNIYLCIAVYLKKVYRRGKPQSI--TMDHMK 205
Cdd:cd14610   205 N---KCYRGRScPIIVHCsdgagRSGTYILIDMVLNKMAKGAKEIDIaaTLEHLR 256

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

2-179

1.70e-41

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: 142.30 E-value: 1.70e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVkltLIDGKQDsgYINANY----IQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCE 77
Cdd:cd14600    43 KNRYKDVLPYDATRV---VLQGNED--YINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  78 EHGKVLCDQYWPS--ETAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFA 155
Cdd:cd14600   118 ERGRTKCHQYWPDppDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEE--RTVTHLQYVAWPDHGVPDDSSDFLEFV 195

                         170       180
                  ....*....|....*....|....
gi 2075913722 156 ELVREEIQITKgpgPTVLHCRNNI 179
Cdd:cd14600   196 NYVRSKRVENE---PVLVHCSAGI 216

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

29-175

1.99e-41

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: 139.87 E-value: 1.99e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPS---ETAAYGPFTVQKVSE 105
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEegeEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075913722 106 -VICKEWTIRHLTINRlkdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVREeiQITKGPGPTVLHC 175
Cdd:cd14542    81 kRVGPDFLIRTLKVTF----QKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD--YQGSEDVPICVHC 145

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

2-194

1.23e-40

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: 140.25 E-value: 1.23e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14629    56 KNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPSETAA-YGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVRE 160
Cdd:cd14629   136 EKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHK 213

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2075913722 161 EIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14629   214 TKEQFGQDGPITVHCsagvgRTGVFITLSIVLERMRYEG 252

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

2-179

4.29e-40

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: 138.18 E-value: 4.29e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTlidgKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:cd14607    27 RNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYWPS---ETAAYGP--FTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:cd14607   103 VKCAQYWPTdeeEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDFGVPESPASFLNFLF 180

                         170       180
                  ....*....|....*....|...
gi 2075913722 157 LVREEIQITKGPGPTVLHCRNNI 179
Cdd:cd14607   181 KVRESGSLSPEHGPAVVHCSAGI 203

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

29-194

4.72e-40

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: 136.65 E-value: 4.72e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE-TAAYGPFTVQKVSEVI 107
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 108 CKEWTIRHLTI--NRLKDVD----SPVRHISQLHYTAWPDRGIPHNPSSLITFaelVREEIQI-TKGPGPTVLHC----- 175
Cdd:cd17668    81 LAYYTVRNFTLrnTKIKKGSqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTF---VRKASYAkRHAVGPVVVHCsagvg 157

                         170
                  ....*....|....*....
gi 2075913722 176 RNNIYLCIAVYLKKVYRRG 194
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEG 176

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

29-175

5.59e-40

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: 136.31 E-value: 5.59e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANY----IQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPS--ETAAYGPFTVQK 102
Cdd:cd14541     2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQITC 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075913722 103 VSE-----VICKEWTIRHLTINRlkdvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVReeiQITKGPG-PTVLHC 175
Cdd:cd14541    82 VSEevtpsFAFREFILTNTNTGE-------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR---QNRVGMVePTVVHC 150

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

29-194

6.11e-40

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: 135.86 E-value: 6.11e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE-TAAYGPFTVQKVSEVI 107
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDgSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 108 CKEWTIR--HLTINRlkdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITkGPGPTVLHC-----RNNIY 180
Cdd:cd14552    81 YEDYTLRdfLVTKGK----GGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCsagagRTGTF 155

                         170
                  ....*....|....
gi 2075913722 181 LCIAVYLKKVYRRG 194
Cdd:cd14552   156 CALSTVLERVKAEG 169

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

29-187

6.80e-40

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: 135.95 E-value: 6.80e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAAYGPFTVQKVSEVIC 108
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 109 KEWTIRHLTINRLkdvDSPVRH-ISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKgpGPTVLHC-----RNNIYLC 182
Cdd:cd14632    81 AEYSVRTFALERR---GYSARHeVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDA--GPVVVHCsagagRTGCYIV 155


                  ....*
gi 2075913722 183 IAVYL 187
Cdd:cd14632   156 LDVML 160

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

4-194

8.91e-40

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: 136.33 E-value: 8.91e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   4 RYSYILPYDHSRVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVL 83
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  84 CDQYWPSE-TAAYGPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVREEi 162
Cdd:cd14623    81 CAQYWPSDgSVSYGDITIELKKEEECESYTVRDLLVTNTRENKS--RQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ- 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2075913722 163 QITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14623   158 QQQSGNHPITVHCsagagRTGTFCALSTVLERVKAEG 194

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

15-194

1.90e-39

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: 135.15 E-value: 1.90e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  15 RVKLTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAA 94
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  95 YGPFTVQKVSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFaeLVREEIQITKGPGPTVLH 174
Cdd:cd14631    81 YGDFKVTCVEMEPLAEYVVRTFTLERRG--YNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVH 156

                         170       180
                  ....*....|....*....|....*
gi 2075913722 175 C-----RNNIYLCIAVYLKKVYRRG 194
Cdd:cd14631   157 CsagagRTGCYIVIDIMLDMAEREG 181

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

29-192

3.73e-39

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: 134.04 E-value: 3.73e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWP----SETAAYGPFTVQK 102
Cdd:cd14538     1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslnKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 103 VSEVICKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVReEIQITkgpGPTVLHC-----RN 177
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKE--TGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-RIHNS---GPIVVHCsagigRT 154

                         170
                  ....*....|....*
gi 2075913722 178 NIYLCIAVYLKKVYR 192
Cdd:cd14538   155 GVLITIDVALGLIER 169

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

29-177

4.86e-39

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: 133.67 E-value: 4.86e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAAYGPFTVQKVSEVIC 108
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075913722 109 KEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKGPG----PTVLHCRN 177
Cdd:cd14558    81 PTYTVRVFEITHLKRKDS--RTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSD 151

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

29-194

5.06e-39

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: 133.50 E-value: 5.06e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAAYGPFTVQKVSEVIC 108
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 109 KEWTIRHLTINRlKDVdSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVReeiqiTKGP---GPTVLHC-----RNNIY 180
Cdd:cd14555    81 AEYVVRTFALER-RGY-HEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-----ASNPpsaGPIVVHCsagagRTGCY 153

                         170
                  ....*....|....
gi 2075913722 181 LCIAVYLKKVYRRG 194
Cdd:cd14555   154 IVIDIMLDMAEREG 167

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

2-179

7.92e-39

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: 133.89 E-value: 7.92e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQD-SGYINANYIQGFSGANE-YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEH 79
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  80 GKVlCDQYWPSETAAYGPFTVQKVSEVICKEWTIRHLTINRlkdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVR 159
Cdd:cd14611    82 NEK-CVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ----GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                         170       180
                  ....*....|....*....|
gi 2075913722 160 EEIQITKGPGPTVLHCRNNI 179
Cdd:cd14611   157 EDRLASPGRGPVVVHCSAGI 176

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

2-179

9.93e-39

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: 134.60 E-value: 9.93e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDgkQD---SGYINANYIQGFSGANE-YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCE 77
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPD--QDdplSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  78 EHGKVlCDQYWPSETAAYGPFTVqKVSEVICKE-WTIRHLTINRlkdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAE 156
Cdd:cd14613   106 EMNEK-CTEYWPEEQVTYEGIEI-TVKQVIHADdYRLRLITLKS----GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                         170       180
                  ....*....|....*....|....
gi 2075913722 157 LVREEIQITK-GPGPTVLHCRNNI 179
Cdd:cd14613   180 EVEEARQQAEpNCGPVIVHCSAGI 203

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

29-179

2.35e-38

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: 132.38 E-value: 2.35e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQ----GFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWP--SETAAYGPFTVQK 102
Cdd:cd14601     2 YINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPepSGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075913722 103 VSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVREeiQITKGPGPTVLHCRNNI 179
Cdd:cd14601    82 HSEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGI 154

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

2-205

6.54e-38

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: 133.24 E-value: 6.54e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDSGYINAN-YIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHG 80
Cdd:cd14609    45 KNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYWPSETAA-YGPFTVQKVSEVI-CKEWTIRHLTinrLKDVDS-PVRHISQLHYTAWPDRGIPHNPSSLITFAEL 157
Cdd:cd14609   125 VKQCDRYWPDEGSSlYHIYEVNLVSEHIwCEDFLVRSFY---LKNVQTqETRTLTQFHFLSWPAEGIPSSTRPLLDFRRK 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2075913722 158 VReeiQITKGPG-PTVLHC-----RNNIYLCIAVYLKKVYRRGKPQSI--TMDHMK 205
Cdd:cd14609   202 VN---KCYRGRScPIIVHCsdgagRTGTYILIDMVLNRMAKGVKEIDIaaTLEHVR 254

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

29-195

5.25e-36

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: 125.80 E-value: 5.25e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETA-AYGPFTVQKVSEVI 107
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 108 CKEWTIRHLTINRLKDV--DSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVREeiQITKGPGPTVLHC-----RNNIY 180
Cdd:cd14551    81 LVDYTTRKFCIQKVNRGigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS--ANPPRAGPIVVHCsagvgRTGTF 158

                         170
                  ....*....|....*
gi 2075913722 181 LCIAVYLKKVYRRGK 195
Cdd:cd14551   159 IVIDAMLDMMHAEGK 173

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

29-175

1.55e-35

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: 125.26 E-value: 1.55e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWP-----SETAAYGPFTVQ 101
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 102 KVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVRE------EIQITKGPG-PTVLH 174
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQS--RTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnQDVAGHNRNpPTLVH 158


                  .
gi 2075913722 175 C 175
Cdd:cd14540   159 C 159

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

29-194

6.42e-34

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: 120.50 E-value: 6.42e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE-TAAYGPFTVQKVSEVI 107
Cdd:cd14622     2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEgSVTHGEITIEIKNDTL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 108 CKEWTIRH--LTINRLKDvdspVRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITkGPGPTVLHC-----RNNIY 180
Cdd:cd14622    82 LETISIRDflVTYNQEKQ----TRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCsagagRTGTF 156

                         170
                  ....*....|....
gi 2075913722 181 LCIAVYLKKVYRRG 194
Cdd:cd14622   157 IALSNILERVKAEG 170

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

29-205

8.28e-34

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: 120.24 E-value: 8.28e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANE-YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSETAA-YGPFTVQKVSEV 106
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEvYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 107 I-CKEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDRGIPHNPSSLITFAELVReeiQITKGPG-PTVLHC-----RNNI 179
Cdd:cd14546    81 IwCDDYLVRSFYLKNLQ--TSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVN---KSYRGRScPIVVHCsdgagRTGT 155

                         170       180
                  ....*....|....*....|....*...
gi 2075913722 180 YLCIAVYLKKVYRRGKPQSI--TMDHMK 205
Cdd:cd14546   156 YILIDMVLNRMAKGAKEIDIaaTLEHLR 183

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

29-175

8.51e-34

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: 120.18 E-value: 8.51e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSG-ANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWPSE---TAAYGPFTVQKVS 104
Cdd:cd14539     1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075913722 105 EVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKG-PGPTVLHC 175
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLS--RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPIVVHC 150

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

29-187

7.28e-32

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: 115.23 E-value: 7.28e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWP---SETAAYGPFTVQKV 103
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 104 SEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAELVREEIQItkgpGPTVLHC-----RNN 178
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGEN--RLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCsagigRAG 154


                  ....*....
gi 2075913722 179 IYLCIAVYL 187
Cdd:cd14596   155 VLICVDVLL 163

PHA02738

hypothetical protein; Provisional

3-175

2.39e-31

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 116.95 E-value: 2.39e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   3 NRYSYILPYDHSRVklTLIDGKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKV 82
Cdd:PHA02738   53 NRYLDAVCFDHSRV--ILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGRE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  83 LCDQYWPS---ETAAYGPFTVQKVSevickewTIRHL----TINRLKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITFA 155
Cdd:PHA02738  131 KCFPYWSDveqGSIRFGKFKITTTQ-------VETHPhyvkSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2075913722 156 --------ELVREEIQI---TKGPGPTVLHC 175
Cdd:PHA02738  204 levrqcqkELAQESLQIghnRLQPPPIVVHC 234

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

29-177

2.72e-30

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: 110.96 E-value: 2.72e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKvLCDQYWPSET-AAYGPFTVQKVSEVI 107
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEGsGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075913722 108 CKEWTIRHLTINRLKDVDSPVRHISQLHYTAWP-DRGIPHNPSSLITFAELVrEEIQITKGPGPTVLHCRN 177
Cdd:cd14556    80 DEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPrDRDTPPSKRALLKLLSEV-EKWQEQSGEGPIVVHCLN 149

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

2-176

6.73e-30

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 112.11 E-value: 6.73e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKltlidgkQDSGYINANYIQGfSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:COG5599    45 LNRFRDIQPYKETALR-------ANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 --VLCDQYWPSEtAAYGPFTVQkvSEVICKEWTIRHLTIN----RLKDVDSPVRHISQLHYTAWPDRGIPhNPSSLITFA 155
Cdd:COG5599   117 pkVKMPVYFRQD-GEYGKYEVS--SELTESIQLRDGIEARtyvlTIKGTGQKKIEIPVLHVKNWPDHGAI-SAEALKNLA 192

                         170       180
                  ....*....|....*....|..
gi 2075913722 156 ELVREEIQITKGP-GPTVLHCR 176
Cdd:COG5599   193 DLIDKKEKIKDPDkLLPVVHCR 214

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

2-175

1.88e-29

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: 111.24 E-value: 1.88e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLtLIDGKQDSGYINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEH 79
Cdd:cd14599    41 RNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  80 GKVLCDQYWPS-----ETAAYGPF--TVQKVSEVICKEWT---IRHLtinrLKDVDSPVRHisqLHYTAWPDRGIPHNPS 149
Cdd:cd14599   120 GRSKSHRYWPKlgskhSSATYGKFkvTTKFRTDSGCYATTglkVKHL----LSGQERTVWH---LQYTDWPDHGCPEEVQ 192

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2075913722 150 SLITFAELVRE---------EIQITKGPgPTVLHC 175
Cdd:cd14599   193 GFLSYLEEIQSvrrhtnsmlDSTKNCNP-PIVVHC 226

PHA02746

protein tyrosine phosphatase; Provisional

2-179

2.07e-29

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 111.66 E-value: 2.07e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTL-----------IDGKQ--------DSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMV 62
Cdd:PHA02746   54 KNRFHDIPCWDHSRVVINAheslkmfdvgdSDGKKievtsednAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLI 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  63 WEKEVRIIVMLTVCEEHGKVlCDQYWPSETA---AYGPFtVQKVSEVICKEWTIRhlTINRLKDVDSPV-RHISQLHYTA 138
Cdd:PHA02746  134 SEHESQVIVSLTDIDDDDEK-CFELWTKEEDselAFGRF-VAKILDIIEELSFTK--TRLMITDKISDTsREIHHFWFPD 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2075913722 139 WPDRGIPHNPSSLITF--------AELVREEIQITKGPGPTVLHCRNNI 179
Cdd:PHA02746  210 WPDNGIPTGMAEFLELinkvneeqAELIKQADNDPQTLGPIVVHCSAGI 258

PHA02742

protein tyrosine phosphatase; Provisional

2-175

3.64e-28

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 108.17 E-value: 3.64e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQDsgYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGK 81
Cdd:PHA02742   55 KCRYPDAPCFDRNRVILKIEDGGDD--FINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGK 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  82 VLCDQYW-PSE--TAAYGPFTVQKVsevicKEWTIRHLTINRLKDVDS---PVRHISQLHYTAWPDRGIPHNPSSLITFA 155
Cdd:PHA02742  133 EACYPYWmPHErgKATHGEFKIKTK-----KIKSFRNYAVTNLCLTDTntgASLDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                         170       180
                  ....*....|....*....|....*....
gi 2075913722 156 ELVREEIQITKGP---------GPTVLHC 175
Cdd:PHA02742  208 LAVREADLKADVDikgenivkePPILVHC 236

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

29-176

7.36e-26

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: 99.32 E-value: 7.36e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKvlCDQYWPS--ETAAYGPFTVQKVSEV 106
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNED--EPIYWPTkeKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075913722 107 ICKEWTIRHLTI------NRLKDVDSPVRHIsqlHYTAWpdrgiPHNPSSLITFAEL---VREEIQITKgpGPTVLHCR 176
Cdd:cd14550    79 HSCLSNEIRLIVrdfileSTQDDYVLEVRQF---QCPSW-----PNPCSPIHTVFELintVQEWAQQRD--GPIVVHDR 147

PHA02747

protein tyrosine phosphatase; Provisional

2-179

1.57e-25

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 101.23 E-value: 1.57e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   2 KNRYSYILPYDHSRVKLTLIDGKQdSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEE-HG 80
Cdd:PHA02747   54 KNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGtNG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  81 KVLCDQYW-PSETAAY--GPFTVQKVSEVICKEWTIRHLTINRLKDVDSpvRHISQLHYTAWPDRGIPHNPSSLITFAEL 157
Cdd:PHA02747  133 EEKCYQYWcLNEDGNIdmEDFRIETLKTSVRAKYILTLIEITDKILKDS--RKISHFQCSEWFEDETPSDHPDFIKFIKI 210

                         170       180       190
                  ....*....|....*....|....*....|
gi 2075913722 158 ---VREEIQITKGP-----GPTVLHCRNNI 179
Cdd:PHA02747  211 idiNRKKSGKLFNPkdallCPIVVHCSDGV 240

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

29-201

2.89e-25

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: 97.92 E-value: 2.89e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGAN--EYIATQAPMPATFDDFWRMVWEKEVRIIVMLT-VCEEHGKVLCDQYWPSETAA---YGPFTVQK 102
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrLVDNYSTAKCADYFPAEENEsreFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 103 VSEVICKE-WTIRHLTINRLKDVDsPVRHISQLHYTAWPDRGIPHNPSSLitfAELVREEIQITKGPGPTVLHC-----R 176
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEE-PPLSVLHIQYPEWPDHGVPKDTRSV---RELLKRLYGIPPSAGPIVVHCsagigR 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2075913722 177 NNIYLCI-------------AVYLKKVYRRGKPQSITM 201
Cdd:cd17658   157 TGAYCTIhntirrilegdmsAVDLSKTVRKFRSQRIGM 194

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

29-211

3.78e-24

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: 95.43 E-value: 3.78e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANE--YIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCDQYWP-----SETAAYGPF--T 99
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFkiT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 100 VQKVSEVICKEWT---IRHLtinrlkdVDSPVRHISQLHYTAWPDRGIPHNPSSLITFAE---LVREEIQIT---KGPGP 170
Cdd:cd14598    81 TRFRTDSGCYATTglkIKHL-------LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEeiqSVRRHTNSTidpKSPNP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2075913722 171 TVL-HCRNNIYLCIAVYLKKVyrrgkpQSITMDHMKM---PTVLD 211
Cdd:cd14598   154 PVLvHCSAGVGRTGVVILSEI------MIACLEHNEMldiPRVLD 192

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

29-177

6.35e-20

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: 83.92 E-value: 6.35e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTvcEEHGKVLCDQYWPSETA-AYGPFTVQKVSEVI 107
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN--EMDAAQLCMQYWPEKTScCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2075913722 108 CKEWTIRHLTINRLKDVDSPVRHISQLHYTAWPD-RGIPHNPSSLITFAE-LVREEIQITKGPGPTVLHCRN 177
Cdd:cd14634    79 DEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAyRDTPPSKRSILKVVRrLEKWQEQYDGREGRTVVHCLN 150

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

29-174

1.11e-19

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

Pssm-ID: 350508 [Multi-domain] Cd Length: 205 Bit Score: 83.19 E-value: 1.11e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTvceEHGKVLCDQ--YWPSETAAYG--PFTVQKVS 104
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQGLAEDEfvYWPSREESMNceAFTVTLIS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2075913722 105 -EVIC---KEWTIRHLTINRLKDVDSpVRHISQLHYTAWPDrgiPHNP-SSLITFAELVREEiQITKGpGPTVLH 174
Cdd:cd17670    78 kDRLClsnEEQIIIHDFILEATQDDY-VLEVRHFQCPKWPN---PDAPiSSTFELINVIKEE-ALTRD-GPTIVH 146

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

29-177

9.69e-16

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: 73.02 E-value: 9.69e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVL-CDQYWP-SETAAYGPFTVQKVS-- 104
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWpCLQYWPePGLQQYGPMEVEFVSgs 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2075913722 105 ---EVICKEWTIRHLTinRLKDVDSPVRHISQLHYTAWpdRGIPHNPSSLITFAELVrEEIQITKGPGPTVLHCRN 177
Cdd:cd14637    81 adeDIVTRLFRVQNIT--RLQEGHLMVRHFQFLRWSAY--RDTPDSKKAFLHLLASV-EKWQRESGEGRTVVHCLN 151

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

29-177

2.25e-15

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: 72.03 E-value: 2.25e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEhgKVLCDQYWPSE-TAAYGPFTVQKVSEVI 107
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP--AQLCPQYWPENgVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075913722 108 CKEWTIRHLTINRLKDVDSPVRHISQLHYTAWPdrGIPHNPSSLITFAELVRE----EIQITKGPGPTVLHCRN 177
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDGYRMVQQFQFLGWP--MYRDTPVSKRSFLKLIRQvdkwQEEYNGGEGRTVVHCLN 150

PHA02740

protein tyrosine phosphatase; Provisional

8-179

3.02e-15

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 73.08 E-value: 3.02e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722   8 ILPYDHSRVKLtlidgKQDSGYINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEhgKVLCDQY 87
Cdd:PHA02740   62 ITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCFNQF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  88 WPSE---TAAYGPFTVQKVsEVICKEWTIrhLTINRLKDVDSPVRHISQLHYTAWPDRGIPHNPSSLITF--------AE 156
Cdd:PHA02740  135 WSLKegcVITSDKFQIETL-EIIIKPHFN--LTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlcAD 211

                         170       180
                  ....*....|....*....|...
gi 2075913722 157 LVREeiQITKGPGPTVLHCRNNI 179
Cdd:PHA02740  212 LEKH--KADGKIAPIIIDCIDGI 232

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

29-174

4.80e-15

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: 70.79 E-value: 4.80e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEEHGKVLCdQYWPS--ETAAYGPFTVQKVSE- 105
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNkdEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075913722 106 VIC----KEWTIRHLTINRLKdvDSPVRHISQLHYTAWPDrgiPHNP-SSLITFAELVREEiqITKGPGPTVLH 174
Cdd:cd17669    80 HKClsneEKLIIQDFILEATQ--DDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEE--AANRDGPMIVH 146

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

29-193

7.54e-15

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: 70.44 E-value: 7.54e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  29 YINANYIQGFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCE-EHGkvlCDQYWPSE-TAAYGPFTVQKVSEV 106
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYWPEEgMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 107 ICKEWTIRHLTINRLKDVDSPVRHISQLHYTAWPD-RGIPHNPSS---LITFAELVREEIQitKGPGPTVLHC-----RN 177
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWAShREVPGSKRSflkLILQVEKWQEECD--EGEGRTIIHClngggRS 155

                         170
                  ....*....|....*.
gi 2075913722 178 NIYLCIAVYLKKVYRR 193
Cdd:cd14636   156 GMFCAISIVCEMIKRQ 171

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

131-206

1.33e-10

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 56.60 E-value: 1.33e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  131 ISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRGKPQSI--TMDH 203
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCsagvgRTGTFVAIDILLQQLEAEAGEVDIfdTVKE 81


                   ...
gi 2075913722  204 MKM 206
Cdd:smart00404  82 LRS 84

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

131-206

1.33e-10

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: 56.60 E-value: 1.33e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  131 ISQLHYTAWPDRGIPHNPSSLITFAELVREEIQITKGPGPTVLHC-----RNNIYLCIAVYLKKVYRRGKPQSI--TMDH 203
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCsagvgRTGTFVAIDILLQQLEAEAGEVDIfdTVKE 81


                   ...
gi 2075913722  204 MKM 206
Cdd:smart00012  82 LRS 84

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

30-189

4.26e-07

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 48.94 E-value: 4.26e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722  30 INANYIQgFSGANEYIATQAPMPATFDDFWRMVWEKEVRIIVMLTVCEE-HGKVLCDQYWPSETaaYGPFTVQK------ 102
Cdd:cd14559    18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDiQRKGLPPYFRQSGT--YGSVTVKSkktgkd 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075913722 103 --VSEVICKEWTirhLTIN-RLKDVDSPVRHIsqlhyTAWPDrgipHNPSS---LITFAELV----REEIQITKGPGPT- 171
Cdd:cd14559    95 elVDGLKADMYN---LKITdGNKTITIPVVHV-----TNWPD----HTAISsegLKELADLVnksaEEKRNFYKSKGSSa 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2075913722 172 ---------VLHCRNNI----YLCIAVYLKK 189
Cdd:cd14559   163 indknkllpVIHCRAGVgrtgQLAAAMELNK 193

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01