NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1207155753|ref|XP_021324253|]
View 

receptor-type tyrosine-protein phosphatase kappa isoform X17 [Danio rerio]

Protein Classification

fibronectin type III domain-containing protein; immunoglobulin domain-containing protein( domain architecture ID 13891800)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain| immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and/or pattern recognition

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 873-1151 1.44e-159

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 cd14633:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 273  Bit Score: 481.85  E-value: 1.44e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  873 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 952
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  953 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1032
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1033 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1112
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155753 1113 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1237-1442 2.22e-154

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: 465.27  E-value: 2.22e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC 1316
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1317 DVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCA 1396
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1397 ISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 1.47e-53

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 184.47  E-value: 1.47e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155753   186 VLSYPC 191
Cdd:smart00137  156 LSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
491-582 6.50e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155753  571 RASTSKGFGPPT 582
Cdd:pfam00041   74 QAVNGGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 201-282 4.36e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 4.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155753   281 NF 282
Cdd:smart00410   80 GT 81
fn3 pfam00041
Fibronectin type III domain;
293-370 2.01e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155753  370 G 370
Cdd:pfam00041   80 G 80
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 873-1151 1.44e-159

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: 481.85  E-value: 1.44e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  873 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 952
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  953 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1032
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1033 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1112
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155753 1113 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1237-1442 2.22e-154

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: 465.27  E-value: 2.22e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC 1316
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1317 DVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCA 1396
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1397 ISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
888-1148 9.80e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 371.99  E-value: 9.80e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   888 GFKEEYESFFEGQSA--SWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 965
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   966 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA---EVYGDFKVTFVEVEPLAEYVVRTFTLERRGF 1042
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1043 NEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1122
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155753  1123 KALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
912-1148 1.56e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 361.94  E-value: 1.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  912 NRTKNRYGNIIAYDHSRVILQPmeDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEP-LAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATG 1067
Cdd:pfam00102   73 LTELEEKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1068 LLSFIRRV-KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 1207155753 1147 LE 1148
Cdd:pfam00102  233 LE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1181-1442 1.86e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.54  E-value: 1.86e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1181 LKDEFQTLNSVTPQPQPedCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLP 1260
Cdd:smart00194    2 LEEEFEKLDRLKPDDES--CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1261 NTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyL 1336
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET--R 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1337 MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAV 1416
Cdd:smart00194  158 TVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ---STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155753  1417 KSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1208-1442 3.08e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.19  E-value: 3.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLiTIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID-- 1285
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1286 LAQGCPQYWPE--EGMLRYGPVQVDCISCSMDC-DVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKRSFLKL 1362
Cdd:pfam00102   80 GREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPDH-GVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1363 ILQVDKWQEECEegDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:pfam00102  157 LRKVRKSSLDGR--SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 866-1146 1.39e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 199.38  E-value: 1.39e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  866 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDAAKKeqNRTKNRYGNIIAYDHSRVILqPMEDDpSS 940
Cdd:PHA02738     6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDF 1017
Cdd:PHA02738    76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1018 KVTFVEVEPLAEYVVRTFTLErRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------MSNPP 1081
Cdd:PHA02738   150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1082 tagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:PHA02738   229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 1.47e-53

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 184.47  E-value: 1.47e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155753   186 VLSYPC 191
Cdd:smart00137  156 LSNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 35-191 1.66e-47

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.17  E-value: 1.66e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   35 CTFDDGPaqCDYQQDPYDDFDWTHVSAQEVPFLPSDL-----PQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCIDFN 108
Cdd:cd06263      1 CDFEDGL--CGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFWpNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:cd06263     79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1207155753  189 YPC 191
Cdd:cd06263    155 GPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 35-191 2.10e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 166.77  E-value: 2.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   35 CTFDDGpAQCDYQQDPYDDFDWTHVSAQEVPFLPS-----DLPQGSYMMVDTSQHDYGEKARLQLPVMKENDT-HCIDFN 108
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFwPNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 1207155753  189 YPC 191
Cdd:pfam00629  156 GPC 158
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
915-1142 1.08e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.64  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  915 KNRYGNIIAYDHSRVilqpMEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 994
Cdd:COG5599     45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  995 LVEVG--RVKCYKYWPDDAEvYGDFKV--TFVEVEPLAEYV-VRTFTLERRGFN-EVREVKQFHFTGWPDHGVPyHATGL 1068
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1069 LSFIRRV----KMSNPPTaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1141
Cdd:COG5599    189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                   .
gi 1207155753 1142 I 1142
Cdd:COG5599    268 L 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1197-1443 4.17e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 113.17  E-value: 4.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1197 PEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGeSSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCT 1276
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1277 SIVMLNEI--DLAQGCPQYW--PEEGMLRYGPVQVDCISCSMdcdviSRLFRICNL--TRPQEG-YLMVRQFQYLGWAgH 1349
Cdd:PHA02742   120 VIVMITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAYEDWP-H 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1350 REVPASKRSFLKLILQVDKWQEECE---EGDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRN 1421
Cdd:PHA02742   194 GGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273

                          250       260
                   ....*....|....*....|..
gi 1207155753 1422 SKPNMVDSPEQYRFCYDLALEF 1443
Cdd:PHA02742   274 QRHNCLSLPQQYIFCYFIVLIF 295
fn3 pfam00041
Fibronectin type III domain;
491-582 6.50e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155753  571 RASTSKGFGPPT 582
Cdd:pfam00041   74 QAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 489-588 2.47e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.05  E-value: 2.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVpllrpplLVSLPWNTSRYNFTLLHPGTTYQF 568
Cdd:cd00063      1 PSP-PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE-------VEVTPGSETSYTLTGLKPGTEYEF 72

                           90       100
                   ....*....|....*....|.
gi 1207155753  569 LIRASTSKGFGPP-TTLNVTT 588
Cdd:cd00063     73 RVRAVNGGGESPPsESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 489-579 8.43e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 8.43e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGI--ITQYEISYSSVHSfdpsvpllrPPLLVSLPWNTSRYNFTLLHPGTTY 566
Cdd:smart00060    1 PSP-PSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1207155753   567 QFLIRASTSKGFG 579
Cdd:smart00060   71 EFRVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 201-282 4.36e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 4.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155753   281 NF 282
Cdd:smart00410   80 GT 81
fn3 pfam00041
Fibronectin type III domain;
293-370 2.01e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155753  370 G 370
Cdd:pfam00041   80 G 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
452-631 2.45e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  452 VVGNLPPNTNVSLKMILTNPEGRKESDETLIQTQEDVPGPVPKEFVRSTPSEDKISLQWKEPLEPNgiITQYEISYSSVH 531
Cdd:COG3401    195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSG 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  532 SFDPSVpllrpplLVSLpwNTSRYNFTLLHPGTTYQFLIRASTSKGF--GPPTTLNVTTNISAPTleeydgseASLNETA 609
Cdd:COG3401    273 DGPFTK-------VATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPA--------APSGLTA 335

                          170       180
                   ....*....|....*....|....*
gi 1207155753  610 TTIT---VLLKPAQAKGAPISAYQI 631
Cdd:COG3401    336 TAVGsssITLSWTASSDADVTGYNV 360
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 291-370 3.49e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   291 PRPIAPPQLLGVGPTYLLIQ-LNANSIFGDGPIILKEVEYRMTSGSWTETHA-VNSPNYKLWHLDPDTEYEIRVL-LTRP 367
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 1207155753   368 GEG 370
Cdd:smart00060   81 GEG 83
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 205-275 4.95e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 43.29  E-value: 4.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753  205 VNAGQNATFQCIATvRDAVNNKLWlqRRNGEDIPVAEKKNINHRKfaaSFRLKEVSSQDQDLYRCVTQSER 275
Cdd:cd20957     13 VDFGRTAVFNCSVT-GNPIHTVLW--MKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 291-383 5.91e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 43.25  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  291 PRPIAPPQLLGVGPTYLLIQLNANSifGDGPIILK-EVEYR-MTSGSWTE--THAVNSPNYKLWHLDPDTEYEIRVLLTR 366
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....*..
gi 1207155753  367 pgEGGTGQPGPALITRT 383
Cdd:cd00063     79 --GGGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
195-277 9.60e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  195 PHFLR-LGDVEVNAGQNATFQCIAT------VRdavnnklWLqrRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLY 267
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTgtpdpeVS-------WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71

                           90
                   ....*....|
gi 1207155753  268 RCVTQSERGS 277
Cdd:pfam07679   72 TCVATNSAGE 81
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1324-1440 7.36e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.41  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1324 RICNLTRPQEGYLMVR-----QFQYLGWAGHRevPASKRSFLKLILQVDKWQEEceegDGRTIIHCLNGGGRSGMFCAis 1398
Cdd:COG2453     28 AVVSLTEEEELLLGLLeeaglEYLHLPIPDFG--APDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA-- 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1207155753 1399 ivCEMIKRQnvVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLA 1440
Cdd:COG2453    100 --AYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 873-1151 1.44e-159

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: 481.85  E-value: 1.44e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  873 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 952
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  953 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1032
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1033 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1112
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155753 1113 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 928-1151 4.52e-157

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: 472.58  E-value: 4.52e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  928 RVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 1007
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1008 PDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIV 1087
Cdd:cd14631     75 PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1088 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd14631    155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1237-1442 2.22e-154

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: 465.27  E-value: 2.22e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC 1316
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1317 DVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCA 1396
Cdd:cd14636     81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1397 ISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14636    161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 942-1151 1.38e-144

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: 438.97  E-value: 1.38e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1021
Cdd:cd14555      1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1022 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYI 1101
Cdd:cd14555     75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1102 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd14555    155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 910-1152 2.79e-138

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: 423.67  E-value: 2.79e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  910 EQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 989
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  990 VMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLL 1069
Cdd:cd14630     75 VMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1070 SFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1149
Cdd:cd14630    155 GFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234


                   ...
gi 1207155753 1150 CLC 1152
Cdd:cd14630    235 CLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 910-1152 1.85e-127

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: 394.46  E-value: 1.85e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  910 EQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 989
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  990 VMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGL 1068
Cdd:cd14553     75 VMMTKLEERSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1069 LSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14553    155 LAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234


                   ....
gi 1207155753 1149 ACLC 1152
Cdd:cd14553    235 AVTC 238
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 942-1152 8.30e-127

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: 391.72  E-value: 8.30e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1021
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1022 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYI 1101
Cdd:cd14632     75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1102 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1152
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1237-1438 4.03e-123

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: 381.37  E-value: 4.03e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL-AQGCPQYWPEEGMLRYGPVQVDCISCSMD 1315
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPkDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1316 CDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECeeGDGRTIIHCLNGGGRSGMFC 1395
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207155753 1396 AISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
888-1148 9.80e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 371.99  E-value: 9.80e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   888 GFKEEYESFFEGQSA--SWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 965
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   966 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA---EVYGDFKVTFVEVEPLAEYVVRTFTLERRGF 1042
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1043 NEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1122
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155753  1123 KALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
912-1148 1.56e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 361.94  E-value: 1.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  912 NRTKNRYGNIIAYDHSRVILQPmeDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEP-LAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATG 1067
Cdd:pfam00102   73 LTELEEKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1068 LLSFIRRV-KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 1207155753 1147 LE 1148
Cdd:pfam00102  233 LE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 872-1152 4.20e-112

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: 354.73  E-value: 4.20e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  872 ADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiw 951
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  952 lyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEY 1030
Cdd:cd14626     79 ----GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATY 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1031 VVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1110
Cdd:cd14626    155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1207155753 1111 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1152
Cdd:cd14626    235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1237-1442 3.48e-111

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: 349.32  E-value: 3.48e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC 1316
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1317 DVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCA 1396
Cdd:cd14634     81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1397 ISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14634    161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 866-1152 1.19e-107

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: 342.46  E-value: 1.19e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  866 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINA 945
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  946 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DAEVYGDFKVTFVEV 1024
Cdd:cd14625     81 NYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSrGTETYGMIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1025 EPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVID 1104
Cdd:cd14625    155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1105 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1152
Cdd:cd14625    235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1237-1442 3.67e-107

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: 338.20  E-value: 3.67e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC 1316
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1317 DVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCA 1396
Cdd:cd14635     81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1397 ISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14635    161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 866-1153 5.16e-107

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: 340.94  E-value: 5.16e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  866 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINA 945
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  946 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DAEVYGDFKVTFVEV 1024
Cdd:cd14624     81 NYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSrGTETYGLIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1025 EPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVID 1104
Cdd:cd14624    155 VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1105 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCG 1153
Cdd:cd14624    235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1237-1442 1.56e-103

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: 328.02  E-value: 1.56e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQG---CPQYWPEEGMLRYGPVQVDCISCS 1313
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSawpCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1314 MDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECeeGDGRTIIHCLNGGGRSGM 1393
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRES--GEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1394 FCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 942-1144 2.03e-98

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: 313.45  E-value: 2.03e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFK 1018
Cdd:cd00047      1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDIT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG 1098
Cdd:cd00047     75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1099 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd00047    155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 942-1144 4.30e-94

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: 301.58  E-value: 4.30e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVT 1020
Cdd:cd14549      1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTL------ERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGA 1094
Cdd:cd14549     75 LLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1095 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14549    155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 917-1143 1.21e-91

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: 295.80  E-value: 1.21e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  917 RYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 996
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIP------GYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  997 EVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFIRR 1074
Cdd:cd14548     75 EKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRL 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155753 1075 VKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14548    153 VRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 862-1157 2.52e-86

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: 283.84  E-value: 2.52e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  862 TGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQ-SASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSS 940
Cdd:cd14621      1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA-EVYGDFKV 1019
Cdd:cd14621     81 DYINASFIN------GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGcWTYGNIRV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLAEYVVRTFTLERRG----FNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAG 1095
Cdd:cd14621    155 SVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1096 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAI 1157
Cdd:cd14621    235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1181-1442 1.86e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 279.54  E-value: 1.86e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1181 LKDEFQTLNSVTPQPQPedCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLP 1260
Cdd:smart00194    2 LEEEFEKLDRLKPDDES--CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1261 NTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyL 1336
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET--R 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1337 MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAV 1416
Cdd:smart00194  158 TVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQ---STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155753  1417 KSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 889-1151 5.03e-85

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: 279.23  E-value: 5.03e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  889 FKEEYEsffEGQSASWDA------AKKEQNRTKNRYGNIIAYDHSRVILQPM--EDDPSSDYINANYIDiwlyrdGYQRP 960
Cdd:cd17667      1 FSEDFE---EVQRCTADMnitaehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVD------GYNKA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  961 SHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEYVVRTFTLER 1039
Cdd:cd17667     72 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1040 -----------RGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD 1108
Cdd:cd17667    152 tkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQ 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1207155753 1109 MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1151
Cdd:cd17667    232 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1208-1442 3.08e-83

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 272.19  E-value: 3.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLiTIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID-- 1285
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1286 LAQGCPQYWPE--EGMLRYGPVQVDCISCSMDC-DVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKRSFLKL 1362
Cdd:pfam00102   80 GREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPDH-GVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1363 ILQVDKWQEECEegDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:pfam00102  157 LRKVRKSSLDGR--SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 888-1143 8.31e-82

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: 270.00  E-value: 8.31e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  888 GFKEEYESF-FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIAT 966
Cdd:cd14543      4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  967 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGFN 1043
Cdd:cd14543     78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGsslRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1044 EVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---------MSNP----PTAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1110
Cdd:cd14543    158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkaMGDRwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1207155753 1111 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14543    238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 912-1146 5.03e-80

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: 263.94  E-value: 5.03e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  912 NRTKNRYGNIIAYDHSRVILQPMEDD-PSSDYINANYIDIWLYRDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACI 989
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIRNENEGPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  990 VMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRG-FNEVREVKQFHFTGWPDHGVPYHAT 1066
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1067 GLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIF 1141
Cdd:cd14544    161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1207155753 1142 IHDAI 1146
Cdd:cd14544    241 IYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 918-1148 1.13e-79

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: 262.18  E-value: 1.13e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  918 YGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE 997
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  998 VGRVKCYKYWPDDA-EVYGDFKVTFVEVEPLAEYVVRTFTLERR---GFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1073
Cdd:cd14620     75 RKEEKCYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1074 RVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14620    155 KVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 916-1143 1.47e-77

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: 255.78  E-value: 1.47e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 994
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIR------GYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  995 LVEvGRVKCYKYWPDDA-EVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1073
Cdd:cd14547     75 LTE-AKEKCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1074 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14547    152 EVEeaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 916-1148 1.12e-76

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: 253.66  E-value: 1.12e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 995
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMP------GYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  996 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1073
Cdd:cd14619     75 MEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1074 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14619    155 LLRqwLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 912-1147 6.76e-76

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: 251.67  E-value: 6.76e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  912 NRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEVGRVKCYKYWPDDAEVygdfKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT 1066
Cdd:cd14554     80 LTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1067 GLLSFIRRVKMSNPP--TAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14554    156 GFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 1207155753 1145 AIL 1147
Cdd:cd14554    236 AAL 238
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 916-1148 2.15e-75

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: 249.73  E-value: 2.15e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQpMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 995
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMP------GYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  996 VEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF--I 1072
Cdd:cd14615     74 VEQGRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1073 RRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14615    154 VREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 942-1147 8.38e-74

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: 244.50  E-value: 8.38e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVT 1020
Cdd:cd17668      1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTLE--------RRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSA 1092
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1093 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1147
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 942-1143 3.06e-73

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: 242.51  E-value: 3.06e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE-VYGDFKVT 1020
Cdd:cd14551      1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTLER--RGFNE--VREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGR 1096
Cdd:cd14551     75 VEDTVVLVDYTTRKFCIQKvnRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155753 1097 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14551    155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 942-1144 4.23e-72

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: 239.84  E-value: 4.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDIwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFKV 1019
Cdd:cd18533      1 YINASYITL-----PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgeYEGEYGDLTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVE--PLAEYVVRTFTLeRRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAG 1095
Cdd:cd18533     76 ELVSEEenDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKreLNDSASLDPPIIVHCSAGVG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155753 1096 RTGCYIVIDIMLDMAER--------EGVVD-IYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd18533    155 RTGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 905-1147 5.26e-72

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: 240.95  E-value: 5.26e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  905 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQE 984
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIP------GYNSPQEYIATQGPLPETRNDFWKMVLQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  985 QSACIVMVTNLVEVGRVKCYKYWP--DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRgfNEVREVKQFHFTGWPDHGVP 1062
Cdd:cd14614     79 KSQIIVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYTAWPDHGVP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1063 Y--HATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYI 1140
Cdd:cd14614    157 TanAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 236


                   ....*..
gi 1207155753 1141 FIHDAIL 1147
Cdd:cd14614    237 FIHQCVQ 243
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 911-1146 1.41e-71

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: 239.92  E-value: 1.41e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  911 QNRTKNRYGNIIAYDHSRVILQPME-DDPSSDYINANYI--DIWLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSA 987
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImpEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  988 CIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRG-FNEVREVKQFHFTGWPDHGVPYH 1064
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGqGNTERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1065 ATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQY 1139
Cdd:cd14605    161 PGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*..
gi 1207155753 1140 IFIHDAI 1146
Cdd:cd14605    241 RFIYMAV 247
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 916-1143 8.09e-71

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: 236.74  E-value: 8.09e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 995
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIP------GNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  996 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTL-ERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFI 1072
Cdd:cd14617     75 VEKGRVKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1073 RRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14617    155 RTVRdyINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 916-1147 8.09e-71

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: 236.76  E-value: 8.09e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 995
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIP------GYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  996 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1073
Cdd:cd14618     75 MENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1074 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1147
Cdd:cd14618    155 LVRehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 905-1148 1.52e-70

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: 237.47  E-value: 1.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  905 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDD-PSSDYINANYIDIWLYRDGyQRPSHYIATQGPVHETVYDFWRMIWQ 983
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQLLGPD-ENAKTYIASQGCLEATVNDFWQMAWQ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  984 EQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNE-VREVKQFHFTGWPDHG 1060
Cdd:cd14606     90 ENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDHG 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1061 VPYHATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQT 1135
Cdd:cd14606    170 VPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|...
gi 1207155753 1136 EEQYIFIHDAILE 1148
Cdd:cd14606    250 EAQYKFIYVAIAQ 262
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 942-1143 8.12e-70

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: 232.80  E-value: 8.12e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDAEVYGDFK 1018
Cdd:cd14557      1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAEYVVRTFTL--ERRGFNEvREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGR 1096
Cdd:cd14557     75 VKINEEKICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155753 1097 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 942-1149 9.12e-70

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: 233.04  E-value: 9.12e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE----VYGDF 1017
Cdd:cd14538      1 YINASHIRIPVGGDTY----HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1018 KVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNppTAGPIVVHCSAGAGRT 1097
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1098 GCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1149
Cdd:cd14538    155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1237-1438 1.64e-69

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: 231.79  E-value: 1.64e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGM--LRYGPVQVDCISC 1312
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgREKCERYWPEEGGkpLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1313 SMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECeegDGRTIIHCLNGGGRSG 1392
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES--REVTHLHYTGWPDHG-VPSSPEDLLALVRRVRKEARKP---NGPIVVHCSAGVGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1393 MFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd00047    155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 941-1149 1.79e-66

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: 223.75  E-value: 1.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDIWLyrdgyqrPSH-----YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-- 1013
Cdd:cd14541      1 DYINANYVNMEI-------PGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETmq 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1014 YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAG 1093
Cdd:cd14541     74 FGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1094 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1149
Cdd:cd14541    154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 867-1148 1.94e-65

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: 223.84  E-value: 1.94e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  867 PAIRVADLLQHINLMKTSDSY-GFKEEYESFF--EGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYI 943
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  944 NANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVygdfKVTFVE 1023
Cdd:cd14628     84 NASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFV 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1024 VEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA--GPIVVHCSAGAGR 1096
Cdd:cd14628    154 VDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1097 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 912-1148 9.37e-65

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: 221.92  E-value: 9.37e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  912 NRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:cd14627     53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEVGRVKCYKYWPDDAEVygdfKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT 1066
Cdd:cd14627    127 LTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1067 GLLSFIRRVKMSNPPTA--GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14627    203 GFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                   ....
gi 1207155753 1145 AILE 1148
Cdd:cd14627    283 AALE 286
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 915-1146 1.56e-63

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: 217.04  E-value: 1.56e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  915 KNRYGNIIAYDHSRVIL-QPMEDDPSSDYINANYIDiwlyrdGY-QRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV 992
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIR------GYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  993 TNLVEVGRvKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFI 1072
Cdd:cd14613    102 TNIEEMNE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1073 RRV---KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:cd14613    179 QEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 942-1146 2.75e-63

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: 214.05  E-value: 2.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-YGDFKVT 1020
Cdd:cd14552      1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA-GPIVVHCSAGAGRTGC 1099
Cdd:cd14552     75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155753 1100 YIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 889-1148 3.45e-63

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: 217.23  E-value: 3.45e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  889 FKEEYESF--FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIdiwlyRDGYQRPSHYIAT 966
Cdd:cd14610     19 LEKEWEALcaYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIAT 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  967 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAE-YVVRTFTLERRGFNE 1044
Cdd:cd14610     94 QGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1045 VREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVK 1123
Cdd:cd14610    174 TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLE 253

                          250       260
                   ....*....|....*....|....*
gi 1207155753 1124 ALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14610    254 HLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 916-1143 4.77e-63

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: 214.39  E-value: 4.77e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  916 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 995
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYIS------GYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  996 VEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFI 1072
Cdd:cd14616     75 FEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFV 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1073 RRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14616    153 KLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 861-1148 1.06e-62

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: 216.13  E-value: 1.06e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  861 QTGQLHPAIRVADLLQHINLMKTSDSYgfkeeyesffegqSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSS 940
Cdd:cd14629     15 KLTQVPPGESVTAMELEFKLLANSKAH-------------TSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVygdfKVT 1020
Cdd:cd14629     82 DYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA--GPIVVHCSAG 1093
Cdd:cd14629    152 YFVVDPMAEynmpqYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqdGPITVHCSAG 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1094 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14629    232 VGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 910-1147 2.48e-62

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: 212.77  E-value: 2.48e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  910 EQNRTKNRYGNIIAYDHSRVilqPMEDDpsSDYINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACI 989
Cdd:cd14597      1 KENRKKNRYKNILPYDTTRV---PLGDE--GGYINASFIKMPVGDEEFV----YIACQGPLPTTVADFWQMVWEQKSTVI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  990 VMVTNLVEVGRVKCYKYWPDDAE----VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHA 1065
Cdd:cd14597     72 AMMTQEVEGGKIKCQRYWPEILGkttmVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1066 TGLLSFIRRvkMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDA 1145
Cdd:cd14597    152 EQLLTFISY--MRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1207155753 1146 IL 1147
Cdd:cd14597    230 IL 231
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 905-1146 4.70e-61

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: 211.33  E-value: 4.70e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  905 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQE 984
Cdd:cd14604     50 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIK------GVYGPKAYIATQGPLANTVIDFWRMIWEY 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  985 QSACIVMVTNLVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRgfNEVREVKQFHFTGWPDHGV 1061
Cdd:cd14604    124 NVAIIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDV 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1062 PYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEE 1137
Cdd:cd14604    202 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKE 280


                   ....*....
gi 1207155753 1138 QYIFIHDAI 1146
Cdd:cd14604    281 QYELVHRAI 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 914-1143 7.74e-61

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: 208.23  E-value: 7.74e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  914 TKNRYGNIIAYDHSRVILQPME-DDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:cd14611      1 TKNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIR------GYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEVGRvKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSF 1071
Cdd:cd14611     75 ITKLKEKNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1072 IRRVKMS--NPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14611    152 MLDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 914-1143 1.79e-60

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: 207.77  E-value: 1.79e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  914 TKNRYGNIIAYDHSRVILQ-PMEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 991
Cdd:cd14612     17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIR------GYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  992 VTNLVEvGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSF 1071
Cdd:cd14612     91 ITKLKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1072 IRRVKMS--NPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14612    168 VAEVEESrqTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 917-1148 1.86e-60

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: 207.20  E-value: 1.86e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  917 RYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 996
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  997 EVGRVKCYKYWPDDAEV-YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV 1075
Cdd:cd14623     75 ERGQEKCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1076 KMSNPPTAG-PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14623    155 QKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 942-1144 1.88e-60

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: 206.09  E-value: 1.88e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1021
Cdd:cd14558      1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1022 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAG------PIVVHCSAGAG 1095
Cdd:cd14558     75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1096 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14558    155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 895-1148 5.24e-60

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: 207.37  E-value: 5.24e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  895 SFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETV 974
Cdd:cd14603     13 AFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIK------GVDGSRAYIATQGPLSHTV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  975 YDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFV-EVEPLAEYVVRTFTLERRgfNEVREVKQF 1051
Cdd:cd14603     87 LDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1052 HFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVD---IYNCVKALRSR 1128
Cdd:cd14603    165 QYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQ 244

                          250       260
                   ....*....|....*....|
gi 1207155753 1129 RINMVQTEEQYIFIHDAILE 1148
Cdd:cd14603    245 RPAAVQTEEQYEFLYHTVAQ 264
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 891-1148 4.02e-58

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: 202.57  E-value: 4.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  891 EEYESF--FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQpMEDDPS-SDYINANYIdiwlyRDGYQRPSHYIATQ 967
Cdd:cd14609     19 KEWQALcaYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLK-AESNPSrSDYINASPI-----IEHDPRMPAYIATQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  968 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAE-YVVRTFTLERRGFNEV 1045
Cdd:cd14609     93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQET 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1046 REVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKA 1124
Cdd:cd14609    173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEH 252

                          250       260
                   ....*....|....*....|....
gi 1207155753 1125 LRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14609    253 VRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 915-1141 4.57e-57

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: 197.23  E-value: 4.57e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  915 KNRYGNIIAYDHSRVILQpmEDDPSSDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 994
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVK--LKQGDNDYINASLVEV----EEAKR--SYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  995 LVEVGRVKCYKYWPDDaEVYG------DFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGL 1068
Cdd:cd14545     73 LMEKGQIKCAQYWPQG-EGNAmifedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAF 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1069 LSFIRRVKMSN--PPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV--VDIYNCVKALRSRRINMVQTEEQYIF 1141
Cdd:cd14545    152 LNFLQKVRESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 915-1148 8.62e-57

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: 196.60  E-value: 8.62e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  915 KNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 994
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIK------GVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  995 LVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEPLAEYVVRTftLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF 1071
Cdd:cd14602     75 EFEMGKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1072 IRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1147
Cdd:cd14602    153 IWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                   .
gi 1207155753 1148 E 1148
Cdd:cd14602    232 E 232
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 907-1147 9.33e-57

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: 198.15  E-value: 9.33e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  907 AKKEQNRTKNRYGNIIAYDHSRVILQPMEDdpssdYINANYIDIWLyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQS 986
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVLQGNED-----YINASYVNMEI--PSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  987 ACIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYH 1064
Cdd:cd14600    108 SLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDD 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1065 ATGLLSFIRRVKmSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14600    188 SSDFLEFVNYVR-SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                   ...
gi 1207155753 1145 AIL 1147
Cdd:cd14600    267 AIL 269
PHA02738 PHA02738
hypothetical protein; Provisional
 866-1146 1.39e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 199.38  E-value: 1.39e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  866 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDAAKKeqNRTKNRYGNIIAYDHSRVILqPMEDDpSS 940
Cdd:PHA02738     6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDF 1017
Cdd:PHA02738    76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1018 KVTFVEVEPLAEYVVRTFTLErRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------MSNPP 1081
Cdd:PHA02738   150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1082 tagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:PHA02738   229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 942-1148 2.12e-56

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: 194.59  E-value: 2.12e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIdiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVT 1020
Cdd:cd14546      1 YINASTI-----YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FV-EVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGC 1099
Cdd:cd14546     76 LVsEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1100 YIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14546    156 YILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1203-1441 4.53e-55

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: 191.97  E-value: 4.53e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1203 ALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1281
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1282 ---NEIDLAQgCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRS 1358
Cdd:cd14554     81 tklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGVPKSGEG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1359 FLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd14554    157 FIDFIGQVHKTKEQFGQ-EGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 1207155753 1439 LAL 1441
Cdd:cd14554    236 AAL 238
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 941-1146 4.99e-55

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: 190.60  E-value: 4.99e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-YGDFKV 1019
Cdd:cd14622      1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAG-PIVVHCSAGAGRTG 1098
Cdd:cd14622     75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1099 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:cd14622    155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 942-1143 6.40e-55

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: 189.94  E-value: 6.40e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFK 1018
Cdd:cd14542      1 YINANFIK------GVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAE-YVVRTFTLERRgfNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRT 1097
Cdd:cd14542     75 ISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1098 GCYIVIDIMLDMAEREGVVD---IYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 942-1148 2.32e-54

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: 189.20  E-value: 2.32e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDIWLyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-----DAEVYGD 1016
Cdd:cd14540      1 YINASHITATV--GGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggehDALTFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1017 FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF------IRRVKMSNPPTAG---PIV 1087
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRHTNQDVAGHNrnpPTL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1088 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14540    157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 1.47e-53

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 184.47  E-value: 1.47e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155753   186 VLSYPC 191
Cdd:smart00137  156 LSNGPC 161
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 907-1146 2.67e-53

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: 187.48  E-value: 2.67e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  907 AKKEQNRTKNRYGNIIAYDHSRVILQPMEDDpssdYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQS 986
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVI----EEAQR--SYILTQGPLPNTCCHFWLMVWQQKT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  987 ACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGV 1061
Cdd:cd14607     89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEdvksyYTVHLLQLENINSGETRTISHFHYTTWPDFGV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1062 PYHATGLLSFIRRVKMSNP--PTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREG--VVDIYNCVKALRSRRINMVQTEE 1137
Cdd:cd14607    169 PESPASFLNFLFKVRESGSlsPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPD 248


                   ....*....
gi 1207155753 1138 QYIFIHDAI 1146
Cdd:cd14607    249 QLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 907-1157 3.05e-53

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: 188.31  E-value: 3.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  907 AKKEQNRTKNRYGNIIAYDHSRVILQpMEDDpssDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQS 986
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLH-QEDN---DYINASLIKM----EEAQR--SYILTQGPLPNTCGHFWEMVWEQKS 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  987 ACIVMVTNLVEVGRVKCYKYWPDDAE---VYGD--FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGV 1061
Cdd:cd14608     90 RGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1062 PYHATGLLSFIRRVKMSNP--PTAGPIVVHCSAGAGRTGCYIVID---IMLDMAEREGVVDIYNCVKALRSRRINMVQTE 1136
Cdd:cd14608    170 PESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 249

                          250       260
                   ....*....|....*....|...
gi 1207155753 1137 EQYIFIHDAILEAC--LCGETAI 1157
Cdd:cd14608    250 DQLRFSYLAVIEGAkfIMGDSSV 272
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 942-1149 1.71e-52

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: 183.41  E-value: 1.71e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV---YGDFK 1018
Cdd:cd14596      1 YINASYITMPVGEEEL----FYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNppTAGPIVVHCSAGAGRTG 1098
Cdd:cd14596     77 LRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1099 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1149
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1237-1437 2.18e-52

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: 182.85  E-value: 2.18e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGPVQVDcISCSM 1314
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErsQNKCAQYWPEDGSVSSGDITVE-LKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1315 DCDVISrlFRICNLTRPQEGYL-MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHCLNGGGRSGM 1393
Cdd:cd14552     80 DYEDYT--LRDFLVTKGKGGSTrTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207155753 1394 FCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCY 198
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 941-1148 3.84e-51

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: 179.76  E-value: 3.84e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  941 DYINANYIDIWLYRDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFK 1018
Cdd:cd14601      1 DYINANYINMEIPSSSIIN--RYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG 1098
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1099 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1237-1438 7.30e-51

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: 178.36  E-value: 7.30e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeiDLAQG----CPQYWPEEGMlRYGPVQVDCISC 1312
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLT--ELKEGdqeqCAQYWGDEKK-TYGDIEVELKDT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1313 SMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGDGRT---IIHCLNGGG 1389
Cdd:cd14558     78 EKSPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKGE-ELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd14558    155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1236-1443 1.37e-49

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: 174.81  E-value: 1.37e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1236 NYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGPVQVDCISCS 1313
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEreQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1314 MdCDVISrlFRICNLTRPQEGYL-MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHCLNGGGRSG 1392
Cdd:cd14622     81 L-LETIS--IRDFLVTYNQEKQTrLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1393 MFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEF 1443
Cdd:cd14622    155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1155-1444 3.02e-48

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: 174.53  E-value: 3.02e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1155 TAIPVCEFKAAYYDMIRIDSQSNSSHLKDEFQTLNSvtPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-E 1233
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLAS--SKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1234 SSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA--QGCPQYWPEEGMLRYGPVQVDCIS 1311
Cdd:cd14628     79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWPAERSARYQYFVVDPMA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1312 CSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRS 1391
Cdd:cd14628    159 EYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1392 GMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1444
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 35-191 1.66e-47

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.17  E-value: 1.66e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   35 CTFDDGPaqCDYQQDPYDDFDWTHVSAQEVPFLPSDL-----PQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCIDFN 108
Cdd:cd06263      1 CDFEDGL--CGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFWpNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:cd06263     79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1207155753  189 YPC 191
Cdd:cd06263    155 GPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 35-191 2.10e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 166.77  E-value: 2.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   35 CTFDDGpAQCDYQQDPYDDFDWTHVSAQEVPFLPS-----DLPQGSYMMVDTSQHDYGEKARLQLPVMKENDT-HCIDFN 108
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFwPNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 1207155753  189 YPC 191
Cdd:pfam00629  156 GPC 158
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 889-1148 2.36e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 172.11  E-value: 2.36e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  889 FKEEYESFFEGQSA-SWDAAKKEQNRTKNRYGNIIAYDHSRVILqPMEDDpSSDYINANYIDiwlyrdGYQRPSHYIATQ 967
Cdd:PHA02742    28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVIL-KIEDG-GDDFINASYVD------GHNAKGRFICTQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  968 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNE 1044
Cdd:PHA02742   100 APLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGA 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1045 VREVKQFHFTGWPDHGVPYHATGLLSFIRRV-----------KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE 1113
Cdd:PHA02742   180 SLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER 259

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1207155753 1114 GVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:PHA02742   260 AIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1155-1444 5.82e-47

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: 170.68  E-value: 5.82e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1155 TAIPVCEFKAAYYDMIRIDSQSNSSHLKDEFQTLnsVTPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-E 1233
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1234 SSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA--QGCPQYWPEEGMLRYGPVQVDCIS 1311
Cdd:cd14627     80 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMgrEKCHQYWPAERSARYQYFVVDPMA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1312 CSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRS 1391
Cdd:cd14627    160 EYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPISVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1392 GMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1444
Cdd:cd14627    236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 911-1148 1.61e-46

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: 169.02  E-value: 1.61e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  911 QNRTKNRYGNIIAYDHSRVILQPMEDDPSSdYINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIV 990
Cdd:cd14599     37 ENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEW----HYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  991 MVTNLVEVGRVKCYKYWPD-----DAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHA 1065
Cdd:cd14599    112 MVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1066 TGLLSF------IRR--------VKMSNPptagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRIN 1131
Cdd:cd14599    192 QGFLSYleeiqsVRRhtnsmldsTKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMF 267

                          250
                   ....*....|....*..
gi 1207155753 1132 MVQTEEQYIFIHDAILE 1148
Cdd:cd14599    268 MIQTIAQYKFVYQVLIQ 284
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 891-1143 2.64e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 169.41  E-value: 2.64e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  891 EEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPV 970
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWID------GFEDDKKFIATQGPF 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  971 HETVYDFWRMIWQEQSACIVMVTNLVEV-GRVKCYKYW---PDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVR 1046
Cdd:PHA02747   103 AETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1047 EVKQFHFTGWPDHGVPYHATGLLSFI------RRVKMS--NPPTA--GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1116
Cdd:PHA02747   183 KISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262

                          250       260
                   ....*....|....*....|....*..
gi 1207155753 1117 DIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:PHA02747   263 CLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1203-1444 3.52e-46

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: 168.37  E-value: 3.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1203 ALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1281
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1282 NEIDLA--QGCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRSF 1359
Cdd:cd14629    128 TKLREMgrEKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWP-EQGVPKTGEGF 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1360 LKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1439
Cdd:cd14629    205 IDFIGQVHKTKEQFGQ-DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRA 283


                   ....*
gi 1207155753 1440 ALEFI 1444
Cdd:cd14629    284 ALEYL 288
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1233-1442 1.53e-45

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: 164.06  E-value: 1.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1233 ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGPVQVDcI 1310
Cdd:cd14623     22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGDITIE-L 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1311 SCSMDCDVISRLFRICNLTRPQEGYlMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHCLNGGGR 1390
Cdd:cd14623    101 KKEEECESYTVRDLLVTNTRENKSR-QIRQFHFHGWP-EVGIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAGR 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1391 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14623    177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 942-1144 2.46e-45

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: 162.58  E-value: 2.46e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVKCYKYWPDDAE-VYGDFKVT 1020
Cdd:cd14556      1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTLER--RGFNEVREVKQFHFTGWPDHG-VPYHATGLLSFIRRV-KMSNPPTAGPIVVHCSAGAGR 1096
Cdd:cd14556     74 FVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1097 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14556    154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
915-1142 1.08e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.64  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  915 KNRYGNIIAYDHSRVilqpMEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 994
Cdd:COG5599     45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  995 LVEVG--RVKCYKYWPDDAEvYGDFKV--TFVEVEPLAEYV-VRTFTLERRGFN-EVREVKQFHFTGWPDHGVPyHATGL 1068
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1069 LSFIRRV----KMSNPPTaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1141
Cdd:COG5599    189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                   .
gi 1207155753 1142 I 1142
Cdd:COG5599    268 L 268
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 942-1143 2.63e-43

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: 156.86  E-value: 2.63e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE-VGRVKCYKYWPDDA---EVYGDF 1017
Cdd:cd17658      1 YINASLVE----TPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEEnesREFGRI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1018 KVTFVEVEplaeyvVRTFTLERRGF----NEVRE----VKQFHFTGWPDHGVPYHATGLLSFIRRVKMSnPPTAGPIVVH 1089
Cdd:cd17658     77 SVTNKKLK------HSQHSITLRVLevqyIESEEpplsVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1090 CSAGAGRTGCYIVID-----IML-DMAeregVVDIYNCVKALRSRRINMVQTEEQYIFIH 1143
Cdd:cd17658    150 CSAGIGRTGAYCTIHntirrILEgDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 942-1144 3.47e-43

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: 156.39  E-value: 3.47e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---AEVYGDFK 1018
Cdd:cd14539      1 YINASLIE-----DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAIT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1019 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---MSNPPTAGPIVVHCSAGAG 1095
Cdd:cd14539     76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1096 RTGCY-IVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1144
Cdd:cd14539    156 RTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 909-1146 1.50e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 155.96  E-value: 1.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  909 KEQNRTKNRYGNIIAYDHSRVILQPME-------------------DDPSSDYINANYIDiwlyrdGYQRPSHYIATQGP 969
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkievtsEDNAENYIHANFVD------GFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  970 VHETVYDFWRMIWQEQSACIVMVTNlVEVGRVKCYKYW--PDDAEV-YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVR 1046
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSR 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1047 EVKQFHFTGWPDHGVPYHATGLLSFIRRVKM----------SNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1116
Cdd:PHA02746   201 EIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV 280

                          250       260       270
                   ....*....|....*....|....*....|
gi 1207155753 1117 DIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:PHA02746   281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1208-1442 1.93e-41

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: 152.94  E-value: 1.93e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL 1286
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1287 AQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCdviSRLFRICNL--TRPQEgylmVRQFQYLGWAGHrEVPASKRSF 1359
Cdd:cd14553     83 RSrvKCDQYWPTRGTETYGLIQVtllDTVELATYT---VRTFALHKNgsSEKRE----VRQFQFTAWPDH-GVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1360 LKLILQVdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1439
Cdd:cd14553    155 LAFLRRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDA 231


                   ...
gi 1207155753 1440 ALE 1442
Cdd:cd14553    232 LLE 234
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1173-1435 4.06e-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: 153.29  E-value: 4.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1173 DSQSNSSHLKDEFQTLNSVtpQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAA-LMDSYRQPA 1250
Cdd:cd14610     11 DHLKNKNRLEKEWEALCAY--QAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1251 AFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI--DLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC-DVISRLFRICN 1327
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCeDFLVRSFYLKN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1328 LTRPQEgyLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKwqeeCEEGDG-RTIIHCLNGGGRSGMFCAISIVC-EMIK 1405
Cdd:cd14610    169 LQTNET--RTVTQFHFLSWNDQG-VPASTRSLLDFRRKVNK----CYRGRScPIIVHCSDGAGRSGTYILIDMVLnKMAK 241

                          250       260       270
                   ....*....|....*....|....*....|
gi 1207155753 1406 RQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14610    242 GAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1213-1435 5.19e-41

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: 150.97  E-value: 5.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1213 RFMDNLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG-- 1289
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQC-MEKGrv 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1290 -CPQYWPE-EGMLRYGPVQVDCISCSMDCDVISRLFRICNltrpQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVd 1367
Cdd:cd14548     80 kCDHYWPFdQDPVYYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLRFVRLV- 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155753 1368 kwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14548    154 --RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1047-1148 5.20e-41

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: 146.35  E-value: 5.20e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1047 EVKQFHFTGWPDHGVPYHATGLLSFIRRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1123
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1207155753  1124 ALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1047-1148 5.20e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 146.35  E-value: 5.20e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1047 EVKQFHFTGWPDHGVPYHATGLLSFIRRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1123
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1207155753  1124 ALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 942-1148 1.56e-40

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: 149.36  E-value: 1.56e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-----DDAEVYGD 1016
Cdd:cd14598      1 YINASHIKVTVGGKEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1017 FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF------IRRVKMSNPPTAG---PIV 1087
Cdd:cd14598     77 FKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSpnpPVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1088 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1202-1437 3.04e-40

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: 150.59  E-value: 3.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1202 IALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1280
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1281 LNEIDlAQG---CPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNL----TRPqegylmVRQFQYLGWAGHrE 1351
Cdd:cd14543    103 TTRVV-ERGrvkCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTetdeSRQ------VTHFQFTSWPDF-G 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1352 VPASKRSFLKLILQVDKWQEECEEGDGRT----------IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRN 1421
Cdd:cd14543    175 VPSSAAALLDFLGEVRQQQALAVKAMGDRwkghppgppiVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRT 254

                          250
                   ....*....|....*.
gi 1207155753 1422 SKPNMVDSPEQYRFCY 1437
Cdd:cd14543    255 QRAFSIQTPDQYYFCY 270
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1237-1437 4.09e-39

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: 144.77  E-value: 4.09e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEG-MLRYGPVQV-----DCI 1310
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEkPLECETFKVtlsgeDHS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1311 SCSMDCDVISRLFRICNltrPQEGY-LMVRQFQYLGWAghrEVPASKRSFLKLILQVDKWqeeCEEGDGRTIIHCLNGGG 1389
Cdd:cd14550     81 CLSNEIRLIVRDFILES---TQDDYvLEVRQFQCPSWP---NPCSPIHTVFELINTVQEW---AQQRDGPIVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1173-1435 6.74e-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: 144.02  E-value: 6.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1173 DSQSNSSHLKDEFQTLNSVtpQPQPEDCSIALLPRNHDKNRFMDNLPPDRC-LPFLITIDGESSNYINAALMDSY--RQP 1249
Cdd:cd14609      9 DHLRNRDRLAKEWQALCAY--QAEPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASPIIEHdpRMP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1250 AaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI--DLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC-DVISRLFRIC 1326
Cdd:cd14609     87 A-YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCeDFLVRSFYLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1327 NLtRPQEGYLMVrQFQYLGWAGHrEVPASKRSFLKLILQVDKwqeeCEEGDGRTII-HCLNGGGRSGMFCAISIVC-EMI 1404
Cdd:cd14609    166 NV-QTQETRTLT-QFHFLSWPAE-GIPSSTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGRTGTYILIDMVLnRMA 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207155753 1405 KRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14609    239 KGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1237-1442 3.92e-37

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: 139.28  E-value: 3.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEGMLrYGPVQVDCISCSM 1314
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRvKCSRYWPDDTEV-YGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1315 DCDVISRLFricnlTRPQEGY---LMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGGGRS 1391
Cdd:cd14555     80 LAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV---KASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1392 GMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1208-1442 5.22e-36

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: 137.08  E-value: 5.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEID 1285
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1286 LAQ-GCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFricnlTRPQEGY---LMVRQFQYLGWAGHrEVPASKRSFLK 1361
Cdd:cd14630     83 VGRvKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTF-----TVQKKGYheiREIRQFHFTSWPDH-GVPCYATGLLG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1362 LILQVdKWQEECEEGDgrTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1441
Cdd:cd14630    156 FVRQV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232


                   .
gi 1207155753 1442 E 1442
Cdd:cd14630    233 E 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1212-1442 7.74e-36

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: 136.48  E-value: 7.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1212 NRFMDNLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG-- 1289
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC-VEQGrt 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1290 -CPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGylMVRQFQYLGWAGHrEVPASKRSFLKLILQVDK 1368
Cdd:cd14615     80 kCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESR--TVRHFHFTSWPDH-GVPETTDLLINFRHLVRE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1369 WQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14615    157 YMKQNPP-NSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1208-1442 8.44e-36

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: 137.86  E-value: 8.44e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL 1286
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1287 AQ--GCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGH--REVPASKRSFLKL 1362
Cdd:cd14626    121 KSrvKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDHgvPEYPTPILAFLRR 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1363 IlqvdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1441
Cdd:cd14626    199 V-------KACNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271


                   .
gi 1207155753 1442 E 1442
Cdd:cd14626    272 E 272
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1212-1435 9.15e-36

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: 135.99  E-value: 9.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1212 NRFMDNLPPDR---CLPflITIDGESSNYINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA 1287
Cdd:cd14547      1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1288 -QGCPQYWPEEGMLRYGPVQVDCIScsmdcdVISRL-FRICNLT-RPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLIL 1364
Cdd:cd14547     79 kEKCAQYWPEEENETYGDFEVTVQS------VKETDgYTVRKLTlKYGGEKRYLKHYWYTSWPDH-KTPEAAQPLLSLVQ 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1365 QVDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14547    152 EVEEARQT-EPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1206-1437 4.35e-35

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: 135.34  E-value: 4.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1206 PRNHDKNRFMDNLPPDR---CLPFLItiDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-L 1281
Cdd:cd14603     28 KENVKKNRYKDILPYDQtrvILSLLQ--EEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaC 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1282 NEIDLA-QGCPQYWP-EEGMLRYGPVQVDCISCS-MDCDVISRLFRI--CNLTRpqegylMVRQFQYLGWAGHrEVPASK 1356
Cdd:cd14603    106 REIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPDH-GIPDSP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1357 RSFLKLILQVDKWQeeceeGDGRT--IIHCLNGGGRSGMFCAISIVCEMIKRQNVVD---VFHAVKSLRNSKPNMVDSPE 1431
Cdd:cd14603    179 DCMLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEE 253


                   ....*.
gi 1207155753 1432 QYRFCY 1437
Cdd:cd14603    254 QYEFLY 259
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1231-1442 4.42e-35

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: 133.61  E-value: 4.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1231 DGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEGMLrYGPVQVD 1308
Cdd:cd14631      9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRvKCYKYWPDDTEV-YGDFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1309 CISCSMDCDVISRLFricnlTRPQEGYLMVR---QFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCL 1385
Cdd:cd14631     88 CVEMEPLAEYVVRTF-----TLERRGYNEIRevkQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCS 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1386 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14631    159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1237-1437 4.46e-35

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: 133.34  E-value: 4.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALM--DSYRQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML---NEIDLAQgCPQYWPEEGMLRYGPVQVDCIS 1311
Cdd:cd14546      1 YINASTIydHDPRNPA-YIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1312 CSMDC-DVISRLFRICNL----TRpqegylMVRQFQYLGWAgHREVPASKRSFLKLILQVDKwqeeCEEGDGRTII-HCL 1385
Cdd:cd14546     79 EHIWCdDYLVRSFYLKNLqtseTR------TVTQFHFLSWP-DEGIPASAKPLLEFRRKVNK----SYRGRSCPIVvHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1386 NGGGRSGMFCAISIVCE-MIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14546    148 DGAGRTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1237-1438 5.19e-35

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: 132.86  E-value: 5.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEGMLRYGPVQVDCISCS 1313
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNL-VERGrrkCDQYWPKEGTETYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1314 MDCDVISRLFRICNL----TRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGG 1389
Cdd:cd14549     80 VLATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAAN---PPGAGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1237-1437 8.55e-35

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: 132.16  E-value: 8.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEG--MLRYGPVQVDCISC 1312
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKkKCERYWPEEGeeQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1313 SMDCDVIsrLFRICNLTRPQEGYlMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSG 1392
Cdd:cd14542     81 KRVGPDF--LIRTLKVTFQKESR-TVYQFHYTAWPDH-GVPSSVDPILDLVRLVRDYQ---GSEDVPICVHCSAGCGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1393 MFCAISIVCEMIKRQNVVD---VFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14542    154 TICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1212-1441 1.61e-34

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: 132.76  E-value: 1.61e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1212 NRFMDNLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeIDLAQG- 1289
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGr 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1290 --CPQYWPEEGM-LRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGYlmVRQFQYLGWAGHR--EVPASKRSFLKLIL 1364
Cdd:cd14618     80 vlCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMAFRELVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1365 QvdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1441
Cdd:cd14618    158 E----HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1205-1444 3.16e-34

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: 133.29  E-value: 3.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1205 LPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE 1283
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1284 IDLAQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCDVISRLFRICNLTRPQegylmVRQFQYLGWAGHrEVPASKRS 1358
Cdd:cd14625    124 LEEKSriKCDQYWPSRGTETYGMIQVtllDTIELATFCVRTFSLHKNGSSEKRE-----VRQFQFTAWPDH-GVPEYPTP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1359 FLKLILQVdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14625    198 FLAFLRRV----KTCNPPDaGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIH 273


                   ....*..
gi 1207155753 1438 DLALEFI 1444
Cdd:cd14625    274 DALLEAV 280
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1218-1442 4.32e-34

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: 131.22  E-value: 4.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1218 LPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYW 1294
Cdd:cd14620      5 LPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQYW 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1295 PEEGMLRYGPVQVDCISCSMDCDVISRLFRI----CNLTRPQEgylMVRQFQYLGWA--GHREVPASKRSFLKLILQVDK 1368
Cdd:cd14620     85 PDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIqpqlPDGCKAPR---LVTQLHFTSWPdfGVPFTPIGMLKFLKKVKSVNP 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1369 WQEeceegdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14620    162 VHA------GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1208-1442 8.38e-34

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: 132.09  E-value: 8.38e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEID 1285
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1286 LAQ-GCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFRIcnLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLIL 1364
Cdd:cd14633    120 VGRvKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155753 1365 QVdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14633    196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1212-1444 4.92e-33

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: 128.47  E-value: 4.92e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1212 NRFMDNLPPDRCLPFLITIDGE-SSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQ-- 1288
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGrv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1289 GCPQYWPeegmLRYGPVQVDCISCSMDCDVISRLFRICNLT---RPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQ 1365
Cdd:cd14619     81 KCEHYWP----LDYTPCTYGHLRVTVVSEEVMENWTVREFLlkqVEEQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155753 1366 VDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1444
Cdd:cd14619    156 LRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1237-1442 1.11e-32

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: 126.32  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-IDLAQ-GCPQYWPEEGMLrYGPVQVDCISCSM 1314
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlVEVGRvKCSKYWPDDSDT-YGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1315 DCDVISRLFricnlTRPQEGYLM---VRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGGGRS 1391
Cdd:cd14632     80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1392 GMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1211-1442 1.25e-32

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: 127.26  E-value: 1.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1211 KNRFMDNLPPDRCLP--FLITIDgESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEIDLA 1287
Cdd:cd14602      1 KNRYKDILPYDHSRVelSLITSD-EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEFEMG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1288 -QGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLIL 1364
Cdd:cd14602     80 kKKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1365 QVDKWQEEceegDGRTI-IHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDSPEQYRFCYDLA 1440
Cdd:cd14602    155 DVRCYQED----DSVPIcIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230


                   ..
gi 1207155753 1441 LE 1442
Cdd:cd14602    231 IE 232
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1205-1444 1.42e-32

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: 128.70  E-value: 1.42e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1205 LPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE 1283
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1284 IDLAQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCDVISRLFRICNLTRPQegylmVRQFQYLGWAGHrEVPASKRS 1358
Cdd:cd14624    124 LEERSrvKCDQYWPSRGTETYGLIQVtllDTVELATYCVRTFALYKNGSSEKRE-----VRQFQFTAWPDH-GVPEHPTP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1359 FLKLILQVdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14624    198 FLAFLRRV----KTCNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273


                   ....*..
gi 1207155753 1438 DLALEFI 1444
Cdd:cd14624    274 DALLEAV 280
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 942-1148 2.73e-32

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: 125.52  E-value: 2.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDAE-VYGDFKVT 1020
Cdd:cd14634      1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTL--ERRGFNEVREVKQFHFTGWPDH-GVPYHATGLLSFIRRVKMSNPP---TAGPIVVHCSAGA 1094
Cdd:cd14634     73 FVSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1095 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14634    153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1208-1433 4.26e-32

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: 127.74  E-value: 4.26e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRC-LPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEID 1285
Cdd:cd14604     57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMaCREFE 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1286 LA-QGCPQYWPE--EGMLRYGPVQVDCISCSMDCDVISR--LFRICNLTRpqegylMVRQFQYLGWAGHrEVPASKRSFL 1360
Cdd:cd14604    137 MGrKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRtlLLEFQNETR------RLYQFHYVNWPDH-DVPSSFDSIL 209

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1361 KLILQVDKWQeecEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDSPEQY 1433
Cdd:cd14604    210 DMISLMRKYQ---EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1197-1435 6.98e-32

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 125.75  E-value: 6.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1197 PEDCSIALLPRnhdKNRFMDNLPPDRCLPFLITIDGES--SNYINAALMDSY-RQPAAFIVTQHPLPNTVKDFWRLVYDY 1273
Cdd:cd14613     17 PKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQE 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1274 GCTSIVMLNEID-LAQGCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGWAGHReV 1352
Cdd:cd14613     94 RSPIIVMITNIEeMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-T 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1353 PASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQ 1432
Cdd:cd14613    168 PDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQ 247


                   ...
gi 1207155753 1433 YRF 1435
Cdd:cd14613    248 YQF 250
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1237-1438 7.64e-32

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: 124.28  E-value: 7.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAalmdSYRQPAA-----FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EIDLAQG-CPQYWPEEGM-LRYGPVQVD 1308
Cdd:cd18533      1 YINA----SYITLPGtsskrYIATQGPLPATIGDFWKMIWQNNVGVIVMLTpLVENGREkCDQYWPSGEYeGEYGDLTVE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1309 CISCSM--DCDVISRLFRicnLTRPQEGYLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCLN 1386
Cdd:cd18533     77 LVSEEEndDGGFIVREFE---LSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELNDSASL-DPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1387 GGGRSGMFCAISIVCEMIKRQNVVD---------VFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1197-1441 1.99e-31

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: 124.18  E-value: 1.99e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1197 PEDCSIallPRNHDKNRFMDNLP-PDR--CLPFLITIDgESSNYINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYD 1272
Cdd:cd14612      7 PEELDI---PGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1273 YGCTSIVMLNEI-DLAQGCPQYWPE-EGmlRYGPVQVDcISCSMDCDVisrlFRICNLT-RPQEGYLMVRQFQYLGWAGH 1349
Cdd:cd14612     83 EECPIIVMITKLkEKKEKCVHYWPEkEG--TYGRFEIR-VQDMKECDG----YTIRDLTiQLEEESRSVKHYWFSSWPDH 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1350 rEVPASKRSFLKLILQVDKwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDS 1429
Cdd:cd14612    156 -QTPESAGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQT 233

                          250
                   ....*....|...
gi 1207155753 1430 PEQYRFCY-DLAL 1441
Cdd:cd14612    234 SEQYQFLHhTLAL 246
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1203-1435 2.25e-31

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: 123.85  E-value: 2.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1203 ALLPRNHDKNRFMDNLPPDRCLPFLITI-DGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1281
Cdd:cd14614      7 ADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1282 NEIDLAQ--GCPQYWP-EEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgylmVRQFQYLGWAGHrEVPASKRS 1358
Cdd:cd14614     87 TQCNEKRrvKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDH-GVPTANAA 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155753 1359 flKLILQ-VDKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14614    162 --ESILQfVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1210-1437 2.37e-31

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: 123.27  E-value: 2.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1210 DKNRFMDNLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI--DLA 1287
Cdd:cd14545      2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmeKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1288 QGCPQYWP----EEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKRSFLKLI 1363
Cdd:cd14545     79 IKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLNFL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1364 LQVdKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV--VDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14545    156 QKV-RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1211-1437 2.96e-31

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: 123.10  E-value: 2.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1211 KNRFMDNLPPDRCLPFLIT--IDGESSNYINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI-DL 1286
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1287 AQGCPQYWPEEGMLrYGPVQVdCISCSMDCDvisrLFRICNLTRPQEGYLM-VRQFQYLGWAGHReVPASKRSFLKLILQ 1365
Cdd:cd14611     82 NEKCVLYWPEKRGI-YGKVEV-LVNSVKECD----NYTIRNLTLKQGSQSRsVKHYWYTSWPDHK-TPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1366 VDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14611    155 VEEDRLA-SPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1237-1437 3.13e-31

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: 121.94  E-value: 3.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEGMLRYGPVQVDCISCSM 1314
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKerKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1315 DCDVISRLF------RICNLTRPQegylMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGG 1388
Cdd:cd14551     81 LVDYTTRKFciqkvnRGIGEKRVR----LVTQFHFTSWPDF-GVPFTPIGMLKFLKKV---KSANPPRAGPIVVHCSAGV 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155753 1389 GRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14551    153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1252-1435 6.49e-31

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: 121.67  E-value: 6.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1252 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEG-MLRYGPVQVDCISCSMDCDVISRLFRICN 1327
Cdd:cd14541     21 YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTL-VERGrvkCHQYWPDLGeTMQFGNLQITCVSEEVTPSFAFREFILTN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1328 LTRPQEGYlmVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEgdgRTIIHCLNGGGRSGMFCAISIVCEMIKRQ 1407
Cdd:cd14541    100 TNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE---PTVVHCSAGIGRTGVLITMETAMCLIEAN 173

                          170       180
                   ....*....|....*....|....*...
gi 1207155753 1408 NVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14541    174 EPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 942-1142 7.35e-31

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: 120.89  E-value: 7.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCykYWPDDAEV--YGDFKV 1019
Cdd:cd14550      1 YINASYLQ------GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVE-----VEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATglLSFIRRVKMSNPPTAGPIVVHCSAGA 1094
Cdd:cd14550     73 TLSGedhscLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGG 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1095 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFI 1142
Cdd:cd14550    151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1181-1442 8.78e-31

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: 123.98  E-value: 8.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1181 LKDEFqtlNSVTPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQHPL 1259
Cdd:cd14621     28 FREEF---NALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1260 PNTVKDFWRLVYDYGCTSIVMLNEIDLAQ--GCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNL-----TRPQ 1332
Cdd:cd14621    105 EETVNDFWRMIWEQNTATIVMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtnKKPQ 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1333 EgylMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEegdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDV 1412
Cdd:cd14621    185 R---LITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDV 257

                          250       260       270
                   ....*....|....*....|....*....|
gi 1207155753 1413 FHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14621    258 YGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1208-1446 2.56e-30

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: 121.03  E-value: 2.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLITIDGE--SSNYINA------ALMDSYRQPA-AFIVTQHPLPNTVKDFWRLVYDYGCTSI 1278
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirneNEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1279 VMLNEiDLAQG---CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFricNLTRPQEGYLM--VRQFQYLGWAGHrEV 1352
Cdd:cd14544     81 VMTTK-EVERGknkCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIreIWHYQYLSWPDH-GV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1353 PASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDS 1429
Cdd:cd14544    156 PSDPGGVLNFLEDVNQRQESLPHA-GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQT 234

                          250
                   ....*....|....*..
gi 1207155753 1430 PEQYRFCYDLALEFIET 1446
Cdd:cd14544    235 EAQYKFIYVAVAQYIET 251
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 942-1148 4.66e-30

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: 118.97  E-value: 4.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMvtnLVEVGRVK-CYKYWPDDAEV-YGDFKV 1019
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQgCPQYWPEEGMLrYGPIQV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLAEYVVRTF-----TLERRGFNEVRevkQFHFTGWPDH-GVPYHATGLLSFIRRVKMSNPPT---AGPIVVHC 1090
Cdd:cd14636     72 ECMSCSMDCDVISRIFricnlTRPQEGYLMVQ---QFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECdegEGRTIIHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155753 1091 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14636    149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1208-1446 1.12e-29

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: 119.35  E-value: 1.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLpfLITIDGE----SSNYINAALM--------DSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGC 1275
Cdd:cd14605      2 NKNKNRYKNILPFDHTR--VVLHDGDpnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1276 TSIVMLN-EIDLAQG-CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFRicnLTRPQEGYL--MVRQFQYLGWAGHr 1350
Cdd:cd14605     80 RVIVMTTkEVERGKSkCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELK---LSKVGQGNTerTVWQYHFRTWPDH- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1351 EVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMV 1427
Cdd:cd14605    156 GVPSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                          250
                   ....*....|....*....
gi 1207155753 1428 DSPEQYRFCYDLALEFIET 1446
Cdd:cd14605    235 QTEAQYRFIYMAVQHYIET 253
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1337-1442 1.58e-29

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 113.61  E-value: 1.58e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1337 MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMI-KRQNVVDVFHA 1415
Cdd:smart00404    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 1207155753  1416 VKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1337-1442 1.58e-29

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: 113.61  E-value: 1.58e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  1337 MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMI-KRQNVVDVFHA 1415
Cdd:smart00012    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 1207155753  1416 VKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 942-1148 7.50e-29

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: 115.56  E-value: 7.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDA-EVYGDFKVT 1020
Cdd:cd14635      1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENGvHRHGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1021 FVEVEPLAEYVVRTFTL--ERRGFNEVREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KMSNPPTAGPIVVHCSAGA 1094
Cdd:cd14635     73 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1095 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1200-1445 9.82e-29

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: 117.43  E-value: 9.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1200 CSIALLPRNHDKNRFMDNLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIV 1279
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1280 MLNEIdLAQG---CPQYWPE----EGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGYLMvrQFQYLGWAGHrEV 1352
Cdd:cd14608     94 MLNRV-MEKGslkCAQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL--HFHYTTWPDF-GV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1353 PASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFC-AISIVCEMIKRQN--VVDVFHAVKSLRNSKPNMVDS 1429
Cdd:cd14608    170 PESPASFLNFLFKVRESGSLSPE-HGPVVVHCSAGIGRSGTFClADTCLLLMDKRKDpsSVDIKKVLLEMRKFRMGLIQT 248

                          250
                   ....*....|....*.
gi 1207155753 1430 PEQYRFCYdlaLEFIE 1445
Cdd:cd14608    249 ADQLRFSY---LAVIE 261
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1212-1437 1.03e-28

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: 115.79  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1212 NRFMDNLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG- 1289
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC-VEKGr 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1290 --CPQYWP-EEGMLRYGPVQVDCISCSMDCDVISRLFRICN---LTRPQegylMVRQFQYLGWAGHrEVPASKRSFLKLI 1363
Cdd:cd14617     80 vkCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSeeqLDAPR----LVRHFHYTVWPDH-GVPETTQSLIQFV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1364 LQVDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd14617    155 RTVRDYINR-TPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1235-1435 2.31e-28

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: 114.62  E-value: 2.31e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1235 SNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEG--MLRYGPVQVDC 1309
Cdd:cd14616     25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC-FEKGrirCHQYWPEDNkpVTVFGDIVITK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1310 ISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGGG 1389
Cdd:cd14616    104 LMEDVQIDWTIRDLKI----ERHGDYMMVRQCNFTSWPEH-GVPESSAPLIHFVKLV---RASRAHDNTPMIVHCSAGVG 175

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1435
Cdd:cd14616    176 RTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1237-1441 2.97e-28

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: 113.55  E-value: 2.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI-DLAQGCPQYWPEEGMlrygPVQVDCISCSM- 1314
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDE----PINCETFKVTLi 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1315 --DCDVISR----LFRICNLTRPQEGYLM-VRQFQYLGWAgHREVPASKRSFLKLILqvdkwQEECEEGDGRTIIHCLNG 1387
Cdd:cd17669     77 aeEHKCLSNeeklIIQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAANRDGPMIVHDEHG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1388 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1441
Cdd:cd17669    151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1237-1441 6.92e-28

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: 112.46  E-value: 6.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQGCPQYWP--EEGM----LRYGPVQVDC 1309
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPsrEESMnceaFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1310 ISCSMDCDVISRLFRicnLTRPQEGYLM-VRQFQYLGWAGHREVPASKRSFLKLIlqvdkwQEECEEGDGRTIIHCLNGG 1388
Cdd:cd17670     81 LCLSNEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIVHDEFGA 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1389 GRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1441
Cdd:cd17670    152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1206-1444 1.37e-27

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: 113.98  E-value: 1.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1206 PRNHDKNRFMDNLPPDRC---LPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN 1282
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1283 EIdLAQG---CPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICN--LTRPQEG-------YLMVRQFQYLGWAgHR 1350
Cdd:cd17667    105 NL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYTQWP-DM 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1351 EVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSP 1430
Cdd:cd17667    183 GVPEYALPVLTFVRRSSAAR---TPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                          250
                   ....*....|....
gi 1207155753 1431 EQYRFCYDLALEFI 1444
Cdd:cd17667    260 EQYIFIHDALLEAI 273
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1237-1438 2.51e-27

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: 110.94  E-value: 2.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAA-FIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLA-QGCPQYWPEE--GMLRYGPVQVDCIS 1311
Cdd:cd14539      1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEkQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1312 CSMDCDVISRLFRICNltRPQEGYLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRS 1391
Cdd:cd14539     81 VRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155753 1392 GMFC-AISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd14539    158 GAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 942-1148 3.16e-27

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: 110.77  E-value: 3.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINAnyidiwLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDA-EVYGDFKV 1019
Cdd:cd14637      1 YINA------ALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLAEYVVRTFTLER--RGFNEVREVKQFHFTGW-PDHGVPYHATGLLSFIRRV-KMSNPPTAGPIVVHCSAGAG 1095
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1096 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1148
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1206-1446 3.49e-27

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: 112.67  E-value: 3.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1206 PRNHDKNRFMDNLPPDRCLPFLITIDGE-------SSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSI 1278
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1279 VMLN-EIDLAQG-CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFRICNLTRpQEGYLMVRQFQYLGWAGHrEVPAS 1355
Cdd:cd14606     96 VMTTrEVEKGRNkCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GVPSE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1356 KRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDSPEQ 1432
Cdd:cd14606    174 PGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252

                          250
                   ....*....|....
gi 1207155753 1433 YRFCYDLALEFIET 1446
Cdd:cd14606    253 YKFIYVAIAQFIET 266
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1197-1443 4.17e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 113.17  E-value: 4.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1197 PEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGeSSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCT 1276
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVR 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1277 SIVMLNEI--DLAQGCPQYW--PEEGMLRYGPVQVDCISCSMdcdviSRLFRICNL--TRPQEG-YLMVRQFQYLGWAgH 1349
Cdd:PHA02742   120 VIVMITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAYEDWP-H 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1350 REVPASKRSFLKLILQVDKWQEECE---EGDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRN 1421
Cdd:PHA02742   194 GGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273

                          250       260
                   ....*....|....*....|..
gi 1207155753 1422 SKPNMVDSPEQYRFCYDLALEF 1443
Cdd:PHA02742   274 QRHNCLSLPQQYIFCYFIVLIF 295
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 942-1147 1.69e-26

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: 108.54  E-value: 1.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYkYWPDDAE--VYGDFKV 1019
Cdd:cd17669      1 YINASYIM------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFKV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLA-----EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATglLSFIRRVKMSNPPTAGPIVVHCSAGA 1094
Cdd:cd17669     74 TLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1095 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1147
Cdd:cd17669    152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1201-1435 6.09e-26

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: 109.17  E-value: 6.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1201 SIALLPRNHDKNRFMDNLPPDRCLPFLitidGESSNYINAALMDSyRQPAA-----FIVTQHPLPNTVKDFWRLVYDYGC 1275
Cdd:cd14600     33 TCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EIPSAnivnkYIATQGPLPHTCAQFWQVVWEQKL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1276 TSIVMLNEIDlAQG---CPQYWPE-EGMLRYGPVQVDCisCSMDCDvISRLFRICNLTRPQEG-YLMVRQFQYLGWAGHr 1350
Cdd:cd14600    108 SLIVMLTTLT-ERGrtkCHQYWPDpPDVMEYGGFRVQC--HSEDCT-IAYVFREMLLTNTQTGeERTVTHLQYVAWPDH- 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1351 EVPASKRSFLKLILQVDKWQEECEEgdgrTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSP 1430
Cdd:cd14600    183 GVPDDSSDFLEFVNYVRSKRVENEP----VLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTS 258


                   ....*
gi 1207155753 1431 EQYRF 1435
Cdd:cd14600    259 SQYKF 263
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1237-1442 6.49e-26

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: 107.07  E-value: 6.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALM------DSYRqpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeIDLAQG---CPQYWPE---EGMLRYGP 1304
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVT-QDVEGGkvkCHRYWPDslnKPLICGGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1305 VQVDCISCSMDCDVISRLFricNLTRPQEGYL-MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWqeeceEGDGRTIIH 1383
Cdd:cd14538     76 LEVSLEKYQSLQDFVIRRI---SLRDKETGEVhHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRI-----HNSGPIVVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155753 1384 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14538    147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1235-1444 8.44e-26

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: 107.16  E-value: 8.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1235 SNYINAALMDSYRQpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML--NEIDLAQGCPQYWP----EEGMLRYGPVQVD 1308
Cdd:cd14540      4 ASHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPtlggEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1309 C-ISCSMDCDVISRLfRICNLTRPQegYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEEC-EEGDGR-----TI 1381
Cdd:cd14540     81 TkFSVSSGCYTTTGL-RVKHTLSGQ--SRTVWHLQYTDWPDH-GCPEDVSGFLDFLEEINSVRRHTnQDVAGHnrnppTL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155753 1382 IHCLNGGGRSG--MFCAISIVCemIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1444
Cdd:cd14540    157 VHCSAGVGRTGvvILADLMLYC--LDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1237-1433 1.57e-25

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: 105.68  E-value: 1.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQ--GCPQYWP--EEGMLRYGPVQVDCISC 1312
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNrnKCAQYWPsmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1313 SMDCDVISRLFRICNlTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSG 1392
Cdd:cd14557     81 KICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRTG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207155753 1393 MFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQY 1433
Cdd:cd14557    156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1237-1437 2.61e-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: 105.24  E-value: 2.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALM--DSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQG---CPQYWP-EEGMLR-YGPVQVDC 1309
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaEENESReFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1310 ISCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLIlqvdKWQEECEEGDGRTIIHCLNGGG 1389
Cdd:cd17658     81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELL----KRLYGIPPSAGPIVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNV--VDVFHAVKSLRNSKPNMVDSPEQYRFCY 1437
Cdd:cd17658    156 RTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1237-1438 2.82e-25

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: 105.06  E-value: 2.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEGMLRYGPVQVDCISCS 1313
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPADGSEEYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1314 MDCDVISRLFRICNLT--------RPQEgyLMVRQFQYLGWAgHREVPASKrsfLKLILQVDKWQEECEEGDGRTIIHCL 1385
Cdd:cd17668     80 VLAYYTVRNFTLRNTKikkgsqkgRPSG--RVVTQYHYTQWP-DMGVPEYT---LPVLTFVRKASYAKRHAVGPVVVHCS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155753 1386 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1438
Cdd:cd17668    154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1196-1435 4.54e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 107.78  E-value: 4.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1196 QPEDCSIA--LLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDY 1273
Cdd:PHA02747    37 KPFDGLIAnfEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQE 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1274 GCTSIVMLNEIDLAQG---CPQYW--PEEGMLRYGPVQVDCISCSMDCDVISRLFRICNltRPQEGYLMVRQFQYLGWAG 1348
Cdd:PHA02747   117 HCSIIVMLTPTKGTNGeekCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1349 HrEVPASKRSFLKLILQVDKWQEECEEGDGR-------TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRN 1421
Cdd:PHA02747   195 D-ETPSDHPDFIKFIKIIDINRKKSGKLFNPkdallcpIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIRE 273

                          250
                   ....*....|....
gi 1207155753 1422 SKPNMVDSPEQYRF 1435
Cdd:PHA02747   274 QRHAGIMNFDDYLF 287
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 942-1147 1.26e-24

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: 103.22  E-value: 1.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  942 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDAEVYG--DFKV 1019
Cdd:cd17670      1 YINASYIM------GYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSREESMNceAFTV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1020 TFVEVEPLA-----EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT-GLLSFIRRVKMSNPptaGPIVVHCSAG 1093
Cdd:cd17670     74 TLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRD---GPTIVHDEFG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1094 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1147
Cdd:cd17670    151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1202-1437 4.55e-24

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: 103.12  E-value: 4.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1202 IALLPRNHDKNRFMDNLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1281
Cdd:cd14607     18 VAKYPENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1282 NEI--DLAQGCPQYWP--EEGMLRYGPV--QVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPAS 1355
Cdd:cd14607     95 NRIveKDSVKCAQYWPtdEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDF-GVPES 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1356 KRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQN--VVDVFHAVKSLRNSKPNMVDSPEQY 1433
Cdd:cd14607    172 PASFLNFLFKVRESGSLSPE-HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQL 250


                   ....
gi 1207155753 1434 RFCY 1437
Cdd:cd14607    251 RFSY 254
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1234-1445 8.56e-24

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: 101.18  E-value: 8.56e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1234 SSNYINAALmDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeIDLAQG---CPQYWPE-EGMLRYGPVQVDC 1309
Cdd:cd14601      4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLT-TQVERGrvkCHQYWPEpSGSSSYGGFQVTC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1310 ISCSMDCDVISRLFRICNLTRPQEGYLMvrQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGGG 1389
Cdd:cd14601     82 HSEEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSAGIG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155753 1390 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1445
Cdd:cd14601    156 RTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1228-1444 7.53e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 101.26  E-value: 7.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1228 ITIDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA-QGCPQYW--PEEGMLRYGP 1304
Cdd:PHA02746    91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDdEKCFELWtkEEDSELAFGR 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1305 VQVDCISCSMDCDVISRLFRICNLTrpQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECE-------EGD 1377
Cdd:PHA02746   171 FVAKILDIIEELSFTKTRLMITDKI--SDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAELIkqadndpQTL 247

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1378 GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYdLALEFI 1444
Cdd:PHA02746   248 GPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKYA 313
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1237-1442 1.31e-21

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: 94.43  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1237 YINAA--LMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EIDLAQ-GCPQYWPE--EGMLRYGPVQVDCI 1310
Cdd:cd14596      1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKvKCHRYWPEtlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1311 SCSMDCDVISRLFRICNltRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEEceegdGRTIIHCLNGGGR 1390
Cdd:cd14596     81 NYQALQYFIIRIIKLVE--KETGENRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAGIGR 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1391 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1442
Cdd:cd14596    153 AGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PHA02738 PHA02738
hypothetical protein; Provisional
 1207-1447 4.71e-21

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 95.76  E-value: 4.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1207 RNHDKNRFMDNLPPDRCLPFLITiDGESSNYINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML--NEI 1284
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVILPA-ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLckKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1285 DLAQGCPQYWP--EEGMLRYGPVQVDCISCSMDCDVISRLFRicnLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKL 1362
Cdd:PHA02738   127 NGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLL---LTDGTSATQTVTHFNFTAWPDH-DVPKNTSEFLNF 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1363 ILQVDKWQEECEE-----GDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQ 1432
Cdd:PHA02738   203 VLEVRQCQKELAQeslqiGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                          250
                   ....*....|....*
gi 1207155753 1433 YRFCYDLALEFIETS 1447
Cdd:PHA02738   283 YFFCYRAVKRYVNLT 297
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1208-1441 2.08e-20

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: 91.82  E-value: 2.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1208 NHDKNRFMDNLPPDRCLPFLitidGESSNYINAAL--MDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEI 1284
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1285 DLAQ-GCPQYWPEEgmLRyGPVQVD---CISCSMDCDVISRLFRICNLTRPQEGYL-MVRQFQYLGWAGHrEVPASKRSF 1359
Cdd:cd14597     79 EGGKiKCQRYWPEI--LG-KTTMVDnrlQLTLVRMQQLKNFVIRVLELEDIQTREVrHITHLNFTAWPDH-DTPSQPEQL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1360 LKLILQVDKWQEEceegdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1439
Cdd:cd14597    155 LTFISYMRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1207155753 1440 AL 1441
Cdd:cd14597    230 IL 231
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1193-1445 2.13e-17

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: 84.28  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1193 PQPQPEDC-SIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDSYRQPAA--FIVTQHPLPNTVKDFWRL 1269
Cdd:cd14599     22 PKKKADGVfTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQM 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1270 VYDYGCTSIVMLNEiDLAQGCPQ---YWPEEGMLR----YGPVQVDC-ISCSMDCDVISRLfRICNLTRPQEGylMVRQF 1341
Cdd:cd14599    102 VWEQGVNVIAMVTA-EEEGGRSKshrYWPKLGSKHssatYGKFKVTTkFRTDSGCYATTGL-KVKHLLSGQER--TVWHL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1342 QYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGDGRT-------IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFH 1414
Cdd:cd14599    178 QYTDWPDH-GCPEEVQGFLSYLEEIQSVRRHTNSMLDSTkncnppiVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPV 256

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1207155753 1415 AVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1445
Cdd:cd14599    257 MLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 869-1146 2.18e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.77  E-value: 2.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  869 IRVADLLQHInlmkTSDSYGFKEEYESffEGQSASWDAAKKEQNrtKNRYGNIIAYDHSRVILQPMEDDPSSDYInanyi 948
Cdd:PHA02740    18 INKPDLLSCI----IKEYRAIVPEHED--EANKACAQAENKAKD--ENLALHITRLLHRRIKLFNDEKVLDARFV----- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  949 diwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVgrvKCY-KYWPDD---AEVYGDFKVTFVEV 1024
Cdd:PHA02740    85 ------DGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKegcVITSDKFQIETLEI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1025 EPLAEYVVRTFTLERRgFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV--------KMSNPPTAGPIVVHCSAGAGR 1096
Cdd:PHA02740   156 IIKPHFNLTLLSLTDK-FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGISS 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1097 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1146
Cdd:PHA02740   235 SAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
fn3 pfam00041
Fibronectin type III domain;
491-582 6.50e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155753  571 RASTSKGFGPPT 582
Cdd:pfam00041   74 QAVNGGGEGPPS 85
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1252-1445 8.08e-14

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: 72.32  E-value: 8.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1252 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EIDLAQGCPQYWPEEG----MLRYGPVQVDC-ISCSMDCDVISRLfR 1324
Cdd:cd14598     18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPRLGsrhnTVTYGRFKITTrFRTDSGCYATTGL-K 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1325 ICNLTRPQEgyLMVRQFQYLGWA--GHREVPASKRSFLKLILQVDKWQEECEEGDGRT---IIHCLNGGGRSGMFCAISI 1399
Cdd:cd14598     97 IKHLLTGQE--RTVWHLQYTDWPehGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNppvLVHCSAGVGRTGVVILSEI 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155753 1400 VCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1445
Cdd:cd14598    175 MIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 489-588 2.47e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 64.05  E-value: 2.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVpllrpplLVSLPWNTSRYNFTLLHPGTTYQF 568
Cdd:cd00063      1 PSP-PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE-------VEVTPGSETSYTLTGLKPGTEYEF 72

                           90       100
                   ....*....|....*....|.
gi 1207155753  569 LIRASTSKGFGPP-TTLNVTT 588
Cdd:cd00063     73 RVRAVNGGGESPPsESVTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 943-1139 1.14e-11

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: 66.27  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  943 INANYIDIwlyrdGYQRPShyIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDaEVYGDFKVTFV 1022
Cdd:cd14559     18 LNANRVQI-----GNKNVA--IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQS-GTYGSVTVKSK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1023 EVEPLA---EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGvPYHATGLLSFIRRVKMS----------------NPPTA 1083
Cdd:cd14559     90 KTGKDElvdGLKADMYNLKITDGNKTITIPVVHVTNWPDHT-AISSEGLKELADLVNKSaeekrnfykskgssaiNDKNK 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155753 1084 GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIyncVKALR-SRRINMVQTEEQY 1139
Cdd:cd14559    169 LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRtSRNGKMVQKDEQL 222
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1051-1144 1.65e-09

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 59.28  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1051 FHFTGWPDHGVPyhATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG----CYIVidIMLDMAEREgvvdiynCVKALR 1126
Cdd:cd14506     79 FYNFGWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLV--YALRMSADQ-------AIRLVR 147

                           90
                   ....*....|....*...
gi 1207155753 1127 SRRINMVQTEEQYIFIHD 1144
Cdd:cd14506    148 SKRPNSIQTRGQVLCVRE 165
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1238-1439 6.00e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 59.21  E-value: 6.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1238 INAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWP--EEGMLRYGPVQVDCIscsmd 1315
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSlkEGCVITSDKFQIETL----- 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1316 cDVISR---LFRICNLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKW--QEECEEGDGRT---IIHCLNG 1387
Cdd:PHA02740   154 -EIIIKphfNLTLLSLTDKFGQAQKISHFQYTAWPAD-GFSHDPDAFIDFFCNIDDLcaDLEKHKADGKIapiIIDCIDG 231

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1388 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1439
Cdd:PHA02740   232 ISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHL 283
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 489-579 8.43e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 8.43e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGI--ITQYEISYSSVHSfdpsvpllrPPLLVSLPWNTSRYNFTLLHPGTTY 566
Cdd:smart00060    1 PSP-PSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1207155753   567 QFLIRASTSKGFG 579
Cdd:smart00060   71 EFRVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 201-282 4.36e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.04  E-value: 4.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155753   281 NF 282
Cdd:smart00410   80 GT 81
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1352-1438 9.93e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 50.34  E-value: 9.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1352 VPASKRSFLKLIlqvdKWQEECEEGDGRTIIHCLNGGGRSGMFCAisivCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPE 1431
Cdd:cd14505     85 VPSDIAQWQELL----EELLSALENGKKVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156


                   ....*..
gi 1207155753 1432 QYRFCYD 1438
Cdd:cd14505    157 QENFLHQ 163
fn3 pfam00041
Fibronectin type III domain;
293-370 2.01e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155753  370 G 370
Cdd:pfam00041   80 G 80
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1084-1144 4.33e-06

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 46.96  E-value: 4.33e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753 1084 GPIVVHCSAGAGRTGCYIVIDIMLDMaeREGVVDIYNCVKALRSRRINmvQTEEQYIFIHD 1144
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGGIP--QTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1056-1144 1.15e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1056 WPDHGVPyHATGLLSFIRRVKMSNPPTaGPIVVHCSAGAGRTG----CYIVidimldmaeREGvVDIYNCVKALRSRRIN 1131
Cdd:COG2453     55 IPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGtvaaAYLV---------LLG-LSAEEALARVRAARPG 122

                           90
                   ....*....|...
gi 1207155753 1132 MVQTEEQYIFIHD 1144
Cdd:COG2453    123 AVETPAQRAFLER 135
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
452-631 2.45e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  452 VVGNLPPNTNVSLKMILTNPEGRKESDETLIQTQEDVPGPVPKEFVRSTPSEDKISLQWKEPLEPNgiITQYEISYSSVH 531
Cdd:COG3401    195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSG 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  532 SFDPSVpllrpplLVSLpwNTSRYNFTLLHPGTTYQFLIRASTSKGF--GPPTTLNVTTNISAPTleeydgseASLNETA 609
Cdd:COG3401    273 DGPFTK-------VATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPA--------APSGLTA 335

                          170       180
                   ....*....|....*....|....*
gi 1207155753  610 TTIT---VLLKPAQAKGAPISAYQI 631
Cdd:COG3401    336 TAVGsssITLSWTASSDADVTGYNV 360
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 291-370 3.49e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753   291 PRPIAPPQLLGVGPTYLLIQ-LNANSIFGDGPIILKEVEYRMTSGSWTETHA-VNSPNYKLWHLDPDTEYEIRVL-LTRP 367
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 1207155753   368 GEG 370
Cdd:smart00060   81 GEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1371-1438 4.15e-05

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 44.26  E-value: 4.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155753 1371 EECEEGDGRTIIHCLNGGGRSGMFCAisivCEMIKRQNvVDVFHAVKSLRNSKPN-MVDSPEQYRFCYD 1438
Cdd:cd14494     50 DQAEKPGEPVLVHCKAGVGRTGTLVA----CYLVLLGG-MSAEEAVRIVRLIRPGgIPQTIEQLDFLIK 113
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 205-275 4.95e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 43.29  E-value: 4.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155753  205 VNAGQNATFQCIATvRDAVNNKLWlqRRNGEDIPVAEKKNINHRKfaaSFRLKEVSSQDQDLYRCVTQSER 275
Cdd:cd20957     13 VDFGRTAVFNCSVT-GNPIHTVLW--MKDGKPLGHSSRVQILSED---VLVIPSVKREDKGMYQCFVRNDG 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 291-383 5.91e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 43.25  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  291 PRPIAPPQLLGVGPTYLLIQLNANSifGDGPIILK-EVEYR-MTSGSWTE--THAVNSPNYKLWHLDPDTEYEIRVLLTR 366
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....*..
gi 1207155753  367 pgEGGTGQPGPALITRT 383
Cdd:cd00063     79 --GGGESPPSESVTVTT 93
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1086-1144 3.37e-04

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 42.64  E-value: 3.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155753 1086 IVVHCSAGAGRTG----CYIvidIMLDM-AEREGVVDIyncVKALRSRRInmvQTEEQYIFIHD 1144
Cdd:cd14505    109 VLIHCKGGLGRTGliaaCLL---LELGDtLDPEQAIAA---VRALRPGAI---QTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1085-1142 8.03e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 8.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155753 1085 PIVVHCSAGAGRTG----CYIVIDIMLDMAEregvvdiynCVKALRSRRINMVQTEEQYIFI 1142
Cdd:cd14504     84 AVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
I-set pfam07679
Immunoglobulin I-set domain;
195-277 9.60e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  195 PHFLR-LGDVEVNAGQNATFQCIAT------VRdavnnklWLqrRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLY 267
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTgtpdpeVS-------WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71

                           90
                   ....*....|
gi 1207155753  268 RCVTQSERGS 277
Cdd:pfam07679   72 TCVATNSAGE 81
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 193-287 1.88e-03

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 38.75  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753  193 KSPHflrlgDVEVNAGQNATFQCIATVRDavNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQ 272
Cdd:cd05763      4 KTPH-----DITIRAGSTARLECAATGHP--TPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQ 76

                           90
                   ....*....|....*
gi 1207155753  273 SERGSGVSNfAGLIV 287
Cdd:cd05763     77 NSAGSISAN-ATLTV 90
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1324-1440 7.36e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.41  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155753 1324 RICNLTRPQEGYLMVR-----QFQYLGWAGHRevPASKRSFLKLILQVDKWQEEceegDGRTIIHCLNGGGRSGMFCAis 1398
Cdd:COG2453     28 AVVSLTEEEELLLGLLeeaglEYLHLPIPDFG--APDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA-- 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1207155753 1399 ivCEMIKRQnvVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLA 1440
Cdd:COG2453    100 --AYLVLLG--LSAEEALARVRAARPGAVETPAQRAFLERFA 137
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH