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Conserved domains on  [gi|1207155729|ref|XP_021324246|]
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receptor-type tyrosine-protein phosphatase kappa isoform X8 [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

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 899-1177 1.80e-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: 482.24  E-value: 1.80e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  899 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 978
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  979 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1058
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1059 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1138
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155729 1139 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1263-1474 7.78e-152

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: 459.11  E-value: 7.78e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCI 1342
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1343 SCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGR 1422
Cdd:cd14636     75 SCSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1423 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14636    155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 7.63e-54

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: 185.24  E-value: 7.63e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155729   186 VLSYPC 191
Cdd:smart00137  156 LSNGPC 161
fn3 pfam00041
Fibronectin type III domain;
491-582 6.65e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155729  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 4.25e-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: 4.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155729   281 NF 282
Cdd:smart00410   80 GT 81
fn3 pfam00041
Fibronectin type III domain;
293-370 2.06e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155729  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 ...
 899-1177 1.80e-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: 482.24  E-value: 1.80e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  899 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 978
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  979 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1058
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1059 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1138
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155729 1139 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1263-1474 7.78e-152

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: 459.11  E-value: 7.78e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCI 1342
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1343 SCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGR 1422
Cdd:cd14636     75 SCSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1423 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14636    155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
914-1174 1.05e-118

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 372.38  E-value: 1.05e-118
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   914 GFKEEYESFFEGQSA--SWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 991
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   992 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA---EVYGDFKVTFVEVEPLAEYVVRTFTLERRGF 1068
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1069 NEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1148
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155729  1149 KALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
938-1174 1.40e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 362.72  E-value: 1.40e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  938 NRTKNRYGNIIAYDHSRVILQPmeDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEP-LAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATG 1093
Cdd:pfam00102   73 LTELEEKGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1094 LLSFIRRV-KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 1207155729 1173 LE 1174
Cdd:pfam00102  233 LE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1207-1474 3.23e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.38  E-value: 3.23e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1207 LKDEFQTLNSVTPQPQPedCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDpseeyqSYRQPAAFIV 1286
Cdd:smart00194    2 LEEEFEKLDRLKPDDES--CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1287 TQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNLTR 1362
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1363 PQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceeGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVV 1442
Cdd:smart00194  154 SET--RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1207155729  1443 DVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1234-1474 4.61e-81

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 266.42  E-value: 4.61e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLiTIDGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1313
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVML 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1314 NEID--LAQGCPQYWPE--EGMLRYGPVQVDCISCSMDC-DVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASK 1388
Cdd:pfam00102   74 TELEekGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPDH-GVPESP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1389 RSFLKLILQVDKWQEECEegDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFC 1468
Cdd:pfam00102  151 NSLLDLLRKVRKSSLDGR--SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1207155729 1469 YDLALE 1474
Cdd:pfam00102  229 YDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 892-1172 1.27e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 199.38  E-value: 1.27e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  892 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDAAKKeqNRTKNRYGNIIAYDHSRVILqPMEDDpSS 966
Cdd:PHA02738     6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDF 1043
Cdd:PHA02738    76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1044 KVTFVEVEPLAEYVVRTFTLErRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------MSNPP 1107
Cdd:PHA02738   150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1108 tagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:PHA02738   229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 7.63e-54

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: 185.24  E-value: 7.63e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155729   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 9.30e-48

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: 167.94  E-value: 9.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   35 CTFDDGPaqCDYQQDPYDDFDWTHVSAQEVPFLPSDL-----PQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCIDFN 108
Cdd:cd06263      1 CDFEDGL--CGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFWpNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:cd06263     79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1207155729  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 1.18e-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: 167.54  E-value: 1.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   35 CTFDDGpAQCDYQQDPYDDFDWTHVSAQEVPFLPS-----DLPQGSYMMVDTSQHDYGEKARLQLPVMKENDT-HCIDFN 108
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFwPNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 1207155729  189 YPC 191
Cdd:pfam00629  156 GPC 158
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
941-1168 1.10e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.64  E-value: 1.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  941 KNRYGNIIAYDHSRVilqpMEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1020
Cdd:COG5599     45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1021 LVEVG--RVKCYKYWPDDAEvYGDFKV--TFVEVEPLAEYV-VRTFTLERRGFN-EVREVKQFHFTGWPDHGVPyHATGL 1094
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1095 LSFIRRV----KMSNPPTaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1167
Cdd:COG5599    189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                   .
gi 1207155729 1168 I 1168
Cdd:COG5599    268 L 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1223-1475 8.21e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 106.62  E-value: 8.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1223 PEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGeSSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLV 1302
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVD------GHNAKGRFICTQAPLEETALDFWQAI 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1303 YDYGCTSIVMLNEI--DLAQGCPQYW--PEEGMLRYGPVQVDCISCSMdcdviSRLFRICNL--TRPQEG-YLMVRQFQY 1375
Cdd:PHA02742   114 FQDQVRVIVMITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAY 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1376 LGWAgHREVPASKRSFLKLILQVDKWQEECE---EGDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHA 1447
Cdd:PHA02742   189 EDWP-HGGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                          250       260
                   ....*....|....*....|....*...
gi 1207155729 1448 VKSLRNSKPNMVDSPEQYRFCYDLALEF 1475
Cdd:PHA02742   268 VRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
fn3 pfam00041
Fibronectin type III domain;
491-582 6.65e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155729  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 2.76e-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: 2.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVpllrpplLVSLPWNTSRYNFTLLHPGTTYQF 568
Cdd:cd00063      1 PSP-PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE-------VEVTPGSETSYTLTGLKPGTEYEF 72

                           90       100
                   ....*....|....*....|.
gi 1207155729  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 9.33e-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: 9.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGI--ITQYEISYSSVHSfdpsvpllrPPLLVSLPWNTSRYNFTLLHPGTTY 566
Cdd:smart00060    1 PSP-PSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1207155729   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 4.25e-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: 4.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155729   281 NF 282
Cdd:smart00410   80 GT 81
fn3 pfam00041
Fibronectin type III domain;
293-370 2.06e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155729  370 G 370
Cdd:pfam00041   80 G 80
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
452-631 2.51e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  452 VVGNLPPNTNVSLKMILTNPEGRKESDETLIQTQEDVPGPVPKEFVRSTPSEDKISLQWKEPLEPNgiITQYEISYSSVH 531
Cdd:COG3401    195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSG 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  532 SFDPSVpllrpplLVSLpwNTSRYNFTLLHPGTTYQFLIRASTSKGF--GPPTTLNVTTNISAPTleeydgseASLNETA 609
Cdd:COG3401    273 DGPFTK-------VATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPA--------APSGLTA 335

                          170       180
                   ....*....|....*....|....*
gi 1207155729  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 3.67e-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: 3.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   291 PRPIAPPQLLGVGPTYLLIQ-LNANSIFGDGPIILKEVEYRMTSGSWTETHA-VNSPNYKLWHLDPDTEYEIRVL-LTRP 367
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 1207155729   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 5.36e-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: 5.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729  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 6.41e-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: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  291 PRPIAPPQLLGVGPTYLLIQLNANSifGDGPIILK-EVEYR-MTSGSWTE--THAVNSPNYKLWHLDPDTEYEIRVLLTR 366
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....*..
gi 1207155729  367 pgEGGTGQPGPALITRT 383
Cdd:cd00063     79 --GGGESPPSESVTVTT 93
I-set pfam07679
Immunoglobulin I-set domain;
195-277 1.00e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  195 PHFLR-LGDVEVNAGQNATFQCIAT------VRdavnnklWLqrRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLY 267
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTgtpdpeVS-------WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71

                           90
                   ....*....|
gi 1207155729  268 RCVTQSERGS 277
Cdd:pfam07679   72 TCVATNSAGE 81
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1356-1472 7.75e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.41  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1356 RICNLTRPQEGYLMVR-----QFQYLGWAGHRevPASKRSFLKLILQVDKWQEEceegDGRTIIHCLNGGGRSGMFCAis 1430
Cdd:COG2453     28 AVVSLTEEEELLLGLLeeaglEYLHLPIPDFG--APDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA-- 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1207155729 1431 ivCEMIKRQnvVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLA 1472
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 ...
 899-1177 1.80e-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: 482.24  E-value: 1.80e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  899 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwl 978
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  979 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVV 1058
Cdd:cd14633     78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1059 RTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1138
Cdd:cd14633    155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1207155729 1139 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd14633    235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 954-1177 1.77e-156

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: 471.81  E-value: 1.77e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  954 RVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 1033
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1034 PDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIV 1113
Cdd:cd14631     75 PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1114 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd14631    155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1263-1474 7.78e-152

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: 459.11  E-value: 7.78e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCI 1342
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1343 SCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGR 1422
Cdd:cd14636     75 SCSMDCDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1423 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14636    155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 968-1177 1.53e-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: 439.35  E-value: 1.53e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1047
Cdd:cd14555      1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1048 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYI 1127
Cdd:cd14555     75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1128 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd14555    155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 936-1178 3.03e-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: 424.05  E-value: 3.03e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  936 EQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 1015
Cdd:cd14630      1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1016 VMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLL 1095
Cdd:cd14630     75 VMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1096 SFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1175
Cdd:cd14630    155 GFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234


                   ...
gi 1207155729 1176 CLC 1178
Cdd:cd14630    235 CLC 237
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 936-1178 1.92e-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: 395.23  E-value: 1.92e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  936 EQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 1015
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1016 VMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGL 1094
Cdd:cd14553     75 VMMTKLEERSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1095 LSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14553    155 LAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234


                   ....
gi 1207155729 1175 ACLC 1178
Cdd:cd14553    235 AVTC 238
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 968-1178 1.21e-126

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: 1.21e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1047
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1048 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYI 1127
Cdd:cd14632     75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1128 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1178
Cdd:cd14632    155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1263-1470 9.87e-121

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: 375.21  E-value: 9.87e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL-AQGCPQYWPEEGMLRYGPVQVDC 1341
Cdd:cd14556      1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPkDQSCPQYWPDEGSGTYGPIQVEF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1342 ISCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECeeGDGRTIIHCLNGGG 1421
Cdd:cd14556     75 VSTTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155729 1422 RSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
914-1174 1.05e-118

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 372.38  E-value: 1.05e-118
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   914 GFKEEYESFFEGQSA--SWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 991
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   992 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA---EVYGDFKVTFVEVEPLAEYVVRTFTLERRGF 1068
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1069 NEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1148
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 1207155729  1149 KALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
938-1174 1.40e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 362.72  E-value: 1.40e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  938 NRTKNRYGNIIAYDHSRVILQPmeDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEP-LAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATG 1093
Cdd:pfam00102   73 LTELEEKGREKCAQYWPEEEGeslEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1094 LLSFIRRV-KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 1207155729 1173 LE 1174
Cdd:pfam00102  233 LE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 898-1178 5.59e-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: 5.59e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  898 ADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiw 977
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  978 lyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEY 1056
Cdd:cd14626     79 ----GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATY 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1057 VVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1136
Cdd:cd14626    155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1207155729 1137 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1178
Cdd:cd14626    235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1263-1474 1.09e-108

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: 342.77  E-value: 1.09e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCI 1342
Cdd:cd14634      1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1343 SCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGR 1422
Cdd:cd14634     75 SADIDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1423 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14634    155 SGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 892-1178 1.77e-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: 1.77e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  892 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINA 971
Cdd:cd14625      1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  972 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DAEVYGDFKVTFVEV 1050
Cdd:cd14625     81 NYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSrGTETYGMIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1051 EPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVID 1130
Cdd:cd14625    155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155729 1131 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1178
Cdd:cd14625    235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 892-1179 6.94e-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: 6.94e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  892 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINA 971
Cdd:cd14624      1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  972 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DAEVYGDFKVTFVEV 1050
Cdd:cd14624     81 NYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSrGTETYGLIQVTLLDT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1051 EPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVID 1130
Cdd:cd14624    155 VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155729 1131 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCG 1179
Cdd:cd14624    235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1263-1474 1.04e-104

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: 331.65  E-value: 1.04e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEGMLRYGPVQVDCI 1342
Cdd:cd14635      1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1343 SCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGR 1422
Cdd:cd14635     75 SADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1423 SGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14635    155 SGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1263-1474 3.03e-101

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: 321.86  E-value: 3.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQG---CPQYWPEEGMLRYGPVQV 1339
Cdd:cd14637      1 YINAALTD------SYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSawpCLQYWPEPGLQQYGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 DCISCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHREVPASKRSFLKLILQVDKWQEECeeGDGRTIIHCLNG 1419
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRES--GEGRTVVHCLNG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1420 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14637    153 GGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 968-1170 1.57e-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: 314.22  E-value: 1.57e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFK 1044
Cdd:cd00047      1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDIT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG 1124
Cdd:cd00047     75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155729 1125 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd00047    155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 968-1170 4.21e-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: 301.96  E-value: 4.21e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVT 1046
Cdd:cd14549      1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTL------ERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGA 1120
Cdd:cd14549     75 LLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1121 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14549    155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 943-1169 1.16e-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: 1.16e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  943 RYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 1022
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIP------GYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1023 EVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFIRR 1100
Cdd:cd14548     75 EKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRL 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1101 VKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14548    153 VRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 888-1183 3.02e-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: 283.45  E-value: 3.02e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  888 TGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQ-SASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSS 966
Cdd:cd14621      1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDA-EVYGDFKV 1045
Cdd:cd14621     81 DYINASFIN------GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGcWTYGNIRV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLAEYVVRTFTLERRG----FNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAG 1121
Cdd:cd14621    155 SVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1122 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAI 1183
Cdd:cd14621    235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 915-1177 5.37e-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: 5.37e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  915 FKEEYEsffEGQSASWDA------AKKEQNRTKNRYGNIIAYDHSRVILQPM--EDDPSSDYINANYIDiwlyrdGYQRP 986
Cdd:cd17667      1 FSEDFE---EVQRCTADMnitaehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVD------GYNKA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  987 SHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVTFVEVEPLAEYVVRTFTLER 1065
Cdd:cd17667     72 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1066 -----------RGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD 1134
Cdd:cd17667    152 tkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQ 231

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1207155729 1135 MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1177
Cdd:cd17667    232 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1207-1474 3.23e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 273.38  E-value: 3.23e-83
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1207 LKDEFQTLNSVTPQPQPedCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDpseeyqSYRQPAAFIV 1286
Cdd:smart00194    2 LEEEFEKLDRLKPDDES--CTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1287 TQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNLTR 1362
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVekGREKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1363 PQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceeGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVV 1442
Cdd:smart00194  154 SET--RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQST---STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                           250       260       270
                    ....*....|....*....|....*....|..
gi 1207155729  1443 DVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:smart00194  228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 914-1169 7.04e-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: 7.04e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  914 GFKEEYESF-FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIAT 992
Cdd:cd14543      4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  993 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGFN 1069
Cdd:cd14543     78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGsslRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1070 EVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---------MSNP----PTAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1136
Cdd:cd14543    158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkaMGDRwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1207155729 1137 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14543    238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1234-1474 4.61e-81

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 266.42  E-value: 4.61e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLiTIDGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1313
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVML 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1314 NEID--LAQGCPQYWPE--EGMLRYGPVQVDCISCSMDC-DVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASK 1388
Cdd:pfam00102   74 TELEekGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGWPDH-GVPESP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1389 RSFLKLILQVDKWQEECEegDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFC 1468
Cdd:pfam00102  151 NSLLDLLRKVRKSSLDGR--SGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1207155729 1469 YDLALE 1474
Cdd:pfam00102  229 YDAILE 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 938-1172 5.27e-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: 5.27e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  938 NRTKNRYGNIIAYDHSRVILQPMEDD-PSSDYINANYIDIWLYRDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACI 1015
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIRNENEGPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1016 VMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRG-FNEVREVKQFHFTGWPDHGVPYHAT 1092
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1093 GLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIF 1167
Cdd:cd14544    161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1207155729 1168 IHDAI 1172
Cdd:cd14544    241 IYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 944-1174 1.18e-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: 1.18e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  944 YGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE 1023
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1024 VGRVKCYKYWPDDA-EVYGDFKVTFVEVEPLAEYVVRTFTLERR---GFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1099
Cdd:cd14620     75 RKEEKCYQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1100 RVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14620    155 KVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 942-1169 1.39e-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: 1.39e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1020
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIR------GYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1021 LVEvGRVKCYKYWPDDA-EVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1099
Cdd:cd14547     75 LTE-AKEKCAQYWPEEEnETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1100 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14547    152 EVEeaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 942-1174 1.17e-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: 1.17e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1021
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMP------GYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1022 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1099
Cdd:cd14619     75 MEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1100 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
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 ...
 938-1173 6.15e-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: 6.15e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  938 NRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEVGRVKCYKYWPDDAEVygdfKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT 1092
Cdd:cd14554     80 LTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1093 GLLSFIRRVKMSNPP--TAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14554    156 GFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                   ...
gi 1207155729 1171 AIL 1173
Cdd:cd14554    236 AAL 238
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 942-1174 2.17e-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: 2.17e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQpMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1021
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMP------GYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1022 VEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF--I 1098
Cdd:cd14615     74 VEQGRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155729 1099 RRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14615    154 VREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 968-1173 7.58e-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: 7.58e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDAEVYGDFKVT 1046
Cdd:cd17668      1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTLE--------RRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSA 1118
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1119 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1173
Cdd:cd17668    155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 968-1169 2.99e-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: 2.99e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE-VYGDFKVT 1046
Cdd:cd14551      1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTLER--RGFNE--VREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGR 1122
Cdd:cd14551     75 VEDTVVLVDYTTRKFCIQKvnRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155729 1123 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14551    155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 968-1170 3.08e-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: 240.23  E-value: 3.08e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDIwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFKV 1045
Cdd:cd18533      1 YINASYITL-----PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgeYEGEYGDLTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVE--PLAEYVVRTFTLeRRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAG 1121
Cdd:cd18533     76 ELVSEEenDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKreLNDSASLDPPIIVHCSAGVG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155729 1122 RTGCYIVIDIMLDMAER--------EGVVD-IYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd18533    155 RTGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 931-1173 4.70e-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: 4.70e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  931 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQE 1010
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIP------GYNSPQEYIATQGPLPETRNDFWKMVLQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1011 QSACIVMVTNLVEVGRVKCYKYWP--DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRgfNEVREVKQFHFTGWPDHGVP 1088
Cdd:cd14614     79 KSQIIVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYTAWPDHGVP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1089 Y--HATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYI 1166
Cdd:cd14614    157 TanAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYI 236


                   ....*..
gi 1207155729 1167 FIHDAIL 1173
Cdd:cd14614    237 FIHQCVQ 243
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 937-1172 1.45e-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: 1.45e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  937 QNRTKNRYGNIIAYDHSRVILQPME-DDPSSDYINANYI--DIWLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSA 1013
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImpEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1014 CIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRG-FNEVREVKQFHFTGWPDHGVPYH 1090
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGqGNTERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1091 ATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQY 1165
Cdd:cd14605    161 PGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*..
gi 1207155729 1166 IFIHDAI 1172
Cdd:cd14605    241 RFIYMAV 247
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 942-1169 5.71e-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: 237.12  E-value: 5.71e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1021
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIP------GNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1022 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTL-ERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFI 1098
Cdd:cd14617     75 VEKGRVKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1099 RRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14617    155 RTVRdyINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 942-1173 8.10e-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: 8.10e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1021
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIP------GYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1022 VEVGRVKCYKYWPDDAE--VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIR 1099
Cdd:cd14618     75 MENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155729 1100 RVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1173
Cdd:cd14618    155 LVRehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 931-1174 1.75e-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: 1.75e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  931 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDD-PSSDYINANYIDIWLYRDGyQRPSHYIATQGPVHETVYDFWRMIWQ 1009
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQLLGPD-ENAKTYIASQGCLEATVNDFWQMAWQ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1010 EQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNE-VREVKQFHFTGWPDHG 1086
Cdd:cd14606     90 ENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDHG 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1087 VPYHATGLLSFIRRV--KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQT 1161
Cdd:cd14606    170 VPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|...
gi 1207155729 1162 EEQYIFIHDAILE 1174
Cdd:cd14606    250 EAQYKFIYVAIAQ 262
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 968-1175 7.02e-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: 7.02e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE----VYGDF 1043
Cdd:cd14538      1 YINASHIRIPVGGDTY----HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1044 KVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNppTAGPIVVHCSAGAGRT 1123
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1124 GCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1175
Cdd:cd14538    155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 968-1169 7.81e-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: 7.81e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDAEVYGDFK 1044
Cdd:cd14557      1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAEYVVRTFTL--ERRGFNEvREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGR 1122
Cdd:cd14557     75 VKINEEKICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155729 1123 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1263-1470 2.43e-67

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: 225.63  E-value: 2.43e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGM--LRYGPVQ 1338
Cdd:cd00047      1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgREKCERYWPEEGGkpLEYGDIT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1339 VDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECeegDGRTIIHCLN 1418
Cdd:cd00047     75 VTLVSEEELSDYTIRTLELSPKGCSES--REVTHLHYTGWPDHG-VPSSPEDLLALVRRVRKEARKP---NGPIVVHCSA 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1419 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd00047    149 GVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 967-1175 1.41e-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: 224.13  E-value: 1.41e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDIWLyrdgyqrPSH-----YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-- 1039
Cdd:cd14541      1 DYINANYVNMEI-------PGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETmq 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1040 YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAG 1119
Cdd:cd14541     74 FGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207155729 1120 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1175
Cdd:cd14541    154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 893-1174 2.28e-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: 2.28e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  893 PAIRVADLLQHINLMKTSDSY-GFKEEYESFF--EGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYI 969
Cdd:cd14628      4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  970 NANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVygdfKVTFVE 1049
Cdd:cd14628     84 NASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQYFV 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1050 VEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA--GPIVVHCSAGAGR 1122
Cdd:cd14628    154 VDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPISVHCSAGVGR 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1123 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14628    234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 938-1174 1.07e-64

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: 221.53  E-value: 1.07e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  938 NRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:cd14627     53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEVGRVKCYKYWPDDAEVygdfKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT 1092
Cdd:cd14627    127 LTKLREMGREKCHQYWPAERSA----RYQYFVVDPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGE 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1093 GLLSFIRRVKMSNPPTA--GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14627    203 GFIDFIGQVHKTKEQFGqdGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                   ....
gi 1207155729 1171 AILE 1174
Cdd:cd14627    283 AALE 286
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 941-1172 1.68e-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: 1.68e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  941 KNRYGNIIAYDHSRVIL-QPMEDDPSSDYINANYIDiwlyrdGY-QRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV 1018
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIR------GYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMI 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1019 TNLVEVGRvKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFI 1098
Cdd:cd14613    102 TNIEEMNE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1099 RRV---KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:cd14613    179 QEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 968-1172 2.82e-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: 2.82e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-YGDFKVT 1046
Cdd:cd14552      1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA-GPIVVHCSAGAGRTGC 1125
Cdd:cd14552     75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155729 1126 YIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 915-1174 3.54e-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: 3.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  915 FKEEYESF--FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIdiwlyRDGYQRPSHYIAT 992
Cdd:cd14610     19 LEKEWEALcaYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIAT 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  993 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAE-YVVRTFTLERRGFNE 1070
Cdd:cd14610     94 QGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNE 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1071 VREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVK 1149
Cdd:cd14610    174 TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLE 253

                          250       260
                   ....*....|....*....|....*
gi 1207155729 1150 ALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14610    254 HLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 942-1169 4.15e-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: 4.15e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  942 NRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1021
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYIS------GYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1022 VEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSFI 1098
Cdd:cd14616     75 FEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFV 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1099 RRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14616    153 KLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 887-1174 1.44e-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: 215.75  E-value: 1.44e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  887 QTGQLHPAIRVADLLQHINLMKTSDSYgfkeeyesffegqSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSS 966
Cdd:cd14629     15 KLTQVPPGESVTAMELEFKLLANSKAH-------------TSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVygdfKVT 1046
Cdd:cd14629     82 DYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA----RYQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTA--GPIVVHCSAG 1119
Cdd:cd14629    152 YFVVDPMAEynmpqYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGqdGPITVHCSAG 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1120 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14629    232 VGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 936-1173 2.45e-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: 2.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  936 EQNRTKNRYGNIIAYDHSRVilqPMEDDpsSDYINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACI 1015
Cdd:cd14597      1 KENRKKNRYKNILPYDTTRV---PLGDE--GGYINASFIKMPVGDEEFV----YIACQGPLPTTVADFWQMVWEQKSTVI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1016 VMVTNLVEVGRVKCYKYWPDDAE----VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHA 1091
Cdd:cd14597     72 AMMTQEVEGGKIKCQRYWPEILGkttmVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1092 TGLLSFIRRvkMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDA 1171
Cdd:cd14597    152 EQLLTFISY--MRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                   ..
gi 1207155729 1172 IL 1173
Cdd:cd14597    230 IL 231
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 931-1172 4.82e-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: 4.82e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  931 DAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQE 1010
Cdd:cd14604     50 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIK------GVYGPKAYIATQGPLANTVIDFWRMIWEY 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1011 QSACIVMVTNLVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRgfNEVREVKQFHFTGWPDHGV 1087
Cdd:cd14604    124 NVAIIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDV 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1088 PYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEE 1163
Cdd:cd14604    202 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKE 280


                   ....*....
gi 1207155729 1164 QYIFIHDAI 1172
Cdd:cd14604    281 QYELVHRAI 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 940-1169 8.09e-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: 207.85  E-value: 8.09e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  940 TKNRYGNIIAYDHSRVILQPME-DDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:cd14611      1 TKNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIR------GYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEVGRvKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSF 1097
Cdd:cd14611     75 ITKLKEKNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1098 IRRVKMS--NPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14611    152 MLDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 940-1169 1.84e-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: 1.84e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  940 TKNRYGNIIAYDHSRVILQ-PMEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1017
Cdd:cd14612     17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIR------GYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1018 VTNLVEvGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGfnEVREVKQFHFTGWPDHGVPYHATGLLSF 1097
Cdd:cd14612     91 ITKLKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1098 IRRVKMS--NPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14612    168 VAEVEESrqTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 943-1174 1.90e-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: 1.90e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  943 RYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 1022
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1023 EVGRVKCYKYWPDDAEV-YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV 1101
Cdd:cd14623     75 ERGQEKCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAV 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1102 KMSNPPTAG-PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14623    155 QKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 968-1170 1.91e-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: 1.91e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTF 1047
Cdd:cd14558      1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVEL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1048 VEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAG------PIVVHCSAGAG 1121
Cdd:cd14558     75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155729 1122 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14558    155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 921-1174 5.38e-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: 5.38e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  921 SFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETV 1000
Cdd:cd14603     13 AFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIK------GVDGSRAYIATQGPLSHTV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1001 YDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFV-EVEPLAEYVVRTFTLERRgfNEVREVKQF 1077
Cdd:cd14603     87 LDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPlqTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1078 HFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVD---IYNCVKALRSR 1154
Cdd:cd14603    165 QYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQ 244

                          250       260
                   ....*....|....*....|
gi 1207155729 1155 RINMVQTEEQYIFIHDAILE 1174
Cdd:cd14603    245 RPAAVQTEEQYEFLYHTVAQ 264
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 917-1174 4.12e-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: 4.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  917 EEYESF--FEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQpMEDDPS-SDYINANYIdiwlyRDGYQRPSHYIATQ 993
Cdd:cd14609     19 KEWQALcaYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLK-AESNPSrSDYINASPI-----IEHDPRMPAYIATQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  994 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVTFVEVEPLAE-YVVRTFTLERRGFNEV 1071
Cdd:cd14609     93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQET 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1072 REVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKA 1150
Cdd:cd14609    173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEH 252

                          250       260
                   ....*....|....*....|....
gi 1207155729 1151 LRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14609    253 VRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 941-1167 4.55e-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: 197.61  E-value: 4.55e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  941 KNRYGNIIAYDHSRVILQpmEDDPSSDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1020
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVK--LKQGDNDYINASLVEV----EEAKR--SYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1021 LVEVGRVKCYKYWPDDaEVYG------DFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGL 1094
Cdd:cd14545     73 LMEKGQIKCAQYWPQG-EGNAmifedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAF 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1095 LSFIRRVKMSN--PPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV--VDIYNCVKALRSRRINMVQTEEQYIF 1167
Cdd:cd14545    152 LNFLQKVRESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 941-1174 6.49e-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: 196.98  E-value: 6.49e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  941 KNRYGNIIAYDHSRVILQPMEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1020
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIK------GVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1021 LVEVGRVKCYKYWP---DDAEVYGDFKVTFVEVEPLAEYVVRTftLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF 1097
Cdd:cd14602     75 EFEMGKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1098 IRRVKMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1173
Cdd:cd14602    153 IWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                   .
gi 1207155729 1174 E 1174
Cdd:cd14602    232 E 232
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 933-1173 1.12e-56

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: 1.12e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  933 AKKEQNRTKNRYGNIIAYDHSRVILQPMEDdpssdYINANYIDIWLyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQS 1012
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVLQGNED-----YINASYVNMEI--PSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1013 ACIVMVTNLVEVGRVKCYKYWPDDAEV--YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYH 1090
Cdd:cd14600    108 SLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDD 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1091 ATGLLSFIRRVKmSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14600    188 SSDFLEFVNYVR-SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                   ...
gi 1207155729 1171 AIL 1173
Cdd:cd14600    267 AIL 269
PHA02738 PHA02738
hypothetical protein; Provisional
 892-1172 1.27e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 199.38  E-value: 1.27e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  892 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDAAKKeqNRTKNRYGNIIAYDHSRVILqPMEDDpSS 966
Cdd:PHA02738     6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDF 1043
Cdd:PHA02738    76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQgsiRFGKF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1044 KVTFVEVEPLAEYVVRTFTLErRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------MSNPP 1107
Cdd:PHA02738   150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1108 tagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
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 ...
 968-1174 1.97e-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: 1.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIdiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-AEVYGDFKVT 1046
Cdd:cd14546      1 YINASTI-----YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FV-EVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTGC 1125
Cdd:cd14546     76 LVsEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1126 YIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14546    156 YILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 967-1172 5.11e-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: 5.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV-YGDFKV 1045
Cdd:cd14622      1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAG-PIVVHCSAGAGRTG 1124
Cdd:cd14622     75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155729 1125 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
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; ...
 968-1169 5.62e-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: 190.33  E-value: 5.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFK 1044
Cdd:cd14542      1 YINANFIK------GVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAE-YVVRTFTLERRgfNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRT 1123
Cdd:cd14542     75 ISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207155729 1124 GCYIVIDIMLDMAEREGVVD---IYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 968-1174 2.02e-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: 2.02e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDIWLyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-----DAEVYGD 1042
Cdd:cd14540      1 YINASHITATV--GGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggehDALTFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1043 FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF------IRRVKMSNPPTAG---PIV 1113
Cdd:cd14540     77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRHTNQDVAGHNrnpPTL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1114 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14540    157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 30-191 7.63e-54

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: 185.24  E-value: 7.63e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729    30 AEKGGCTFDDGPaQCDYQQDPYDDFDWTHVSAQE---VPFLPSDLPQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCI 105
Cdd:smart00137    1 TSPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATgipGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   106 DFNYLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTfWPNEYQVIFEAEVTNGRRGFIAIDDIQ 185
Cdd:smart00137   80 TFWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDIL 155


                    ....*.
gi 1207155729   186 VLSYPC 191
Cdd:smart00137  156 LSNGPC 161
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 933-1183 3.13e-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: 3.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  933 AKKEQNRTKNRYGNIIAYDHSRVILQpMEDDpssDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQS 1012
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLH-QEDN---DYINASLIKM----EEAQR--SYILTQGPLPNTCGHFWEMVWEQKS 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1013 ACIVMVTNLVEVGRVKCYKYWPDDAE---VYGD--FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGV 1087
Cdd:cd14608     90 RGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGV 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1088 PYHATGLLSFIRRVKMSNP--PTAGPIVVHCSAGAGRTGCYIVID---IMLDMAEREGVVDIYNCVKALRSRRINMVQTE 1162
Cdd:cd14608    170 PESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTA 249

                          250       260
                   ....*....|....*....|...
gi 1207155729 1163 EQYIFIHDAILEAC--LCGETAI 1183
Cdd:cd14608    250 DQLRFSYLAVIEGAkfIMGDSSV 272
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 933-1172 3.14e-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: 3.14e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  933 AKKEQNRTKNRYGNIIAYDHSRVILQPMEDDpssdYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQS 1012
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVI----EEAQR--SYILTQGPLPNTCCHFWLMVWQQKT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1013 ACIVMVTNLVEVGRVKCYKYWPDDAEVYGDFKVTFVEVEPLAE-----YVVRTFTLERRGFNEVREVKQFHFTGWPDHGV 1087
Cdd:cd14607     89 KAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEdvksyYTVHLLQLENINSGETRTISHFHYTTWPDFGV 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1088 PYHATGLLSFIRRVKMSNP--PTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREG--VVDIYNCVKALRSRRINMVQTEE 1163
Cdd:cd14607    169 PESPASFLNFLFKVRESGSlsPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPD 248


                   ....*....
gi 1207155729 1164 QYIFIHDAI 1172
Cdd:cd14607    249 QLRFSYMAV 257
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1229-1473 7.88e-53

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: 185.42  E-value: 7.88e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1229 ALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGC 1307
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNS 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1308 TSIVML---NEIDLAQgCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREV 1384
Cdd:cd14554     75 TIIVMLtklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGV 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQ 1464
Cdd:cd14554    151 PKSGEGFIDFIGQVHKTKEQFGQ-EGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQ 229


                   ....*....
gi 1207155729 1465 YRFCYDLAL 1473
Cdd:cd14554    230 YQFCYRAAL 238
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 968-1175 1.47e-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: 1.47e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAEV---YGDFK 1044
Cdd:cd14596      1 YINASYITMPVGEEEL----FYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNppTAGPIVVHCSAGAGRTG 1124
Cdd:cd14596     77 LRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1125 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1175
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 967-1174 3.64e-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: 3.64e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  967 DYINANYIDIWLYRDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DAEVYGDFK 1044
Cdd:cd14601      1 DYINANYINMEIPSSSIIN--RYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG 1124
Cdd:cd14601     79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1125 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1263-1469 4.30e-50

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: 176.31  E-value: 4.30e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGPVQVD 1340
Cdd:cd14552      1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErsQNKCAQYWPEDGSVSSGDITVE 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1341 cISCSMDCDVISrlFRICNLTRPQEGYL-MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHCLNG 1419
Cdd:cd14552     75 -LKDQTDYEDYT--LRDFLVTKGKGGSTrTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1420 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14552    149 AGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCY 198
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1263-1470 1.42e-48

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: 171.81  E-value: 1.42e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeiDLAQG----CPQYWPEEGMlRYGPVQ 1338
Cdd:cd14558      1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLT--ELKEGdqeqCAQYWGDEKK-TYGDIE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1339 VDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGDGRT---IIH 1415
Cdd:cd14558     72 VELKDTEKSPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKGE-ELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14558    149 CSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 35-191 9.30e-48

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: 167.94  E-value: 9.30e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   35 CTFDDGPaqCDYQQDPYDDFDWTHVSAQEVPFLPSDL-----PQGSYMMVDTSQHDYGEKARLQLPVMKEN-DTHCIDFN 108
Cdd:cd06263      1 CDFEDGL--CGWTQDSTDDFDWTRVSGSTPSPGTPPDhthgtGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFWpNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:cd06263     79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1207155729  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 1.18e-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: 167.54  E-value: 1.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   35 CTFDDGpAQCDYQQDPYDDFDWTHVSAQEVPFLPS-----DLPQGSYMMVDTSQHDYGEKARLQLPVMKENDT-HCIDFN 108
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPSVKTGPSsdhtqGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  109 YLLYcpdGSSPGTLNVLVKVNKGPLANPIWNITACTGKDWMKAELAVSTFwPNEYQVIFEAEVTNGRRGFIAIDDIQVLS 188
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 1207155729  189 YPC 191
Cdd:pfam00629  156 GPC 158
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 915-1174 2.62e-47

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 172.11  E-value: 2.62e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  915 FKEEYESFFEGQSA-SWDAAKKEQNRTKNRYGNIIAYDHSRVILqPMEDDpSSDYINANYIDiwlyrdGYQRPSHYIATQ 993
Cdd:PHA02742    28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVIL-KIEDG-GDDFINASYVD------GHNAKGRFICTQ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  994 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDAE---VYGDFKVTFVEVEPLAEYVVRTFTLERRGFNE 1070
Cdd:PHA02742   100 APLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGA 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1071 VREVKQFHFTGWPDHGVPYHATGLLSFIRRV-----------KMSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE 1139
Cdd:PHA02742   180 SLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER 259

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1207155729 1140 GVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:PHA02742   260 AIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1262-1475 2.69e-47

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: 168.26  E-value: 2.69e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1262 NYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGPVQV 1339
Cdd:cd14622      1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEreQEKCVQYWPSEGSVTHGEITI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 DCISCSMdCDVISrlFRICNLTRPQEGYL-MVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHCLN 1418
Cdd:cd14622     75 EIKNDTL-LETIS--IRDFLVTYNQEKQTrLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSA 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1419 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEF 1475
Cdd:cd14622    149 GAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 937-1174 1.95e-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: 1.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  937 QNRTKNRYGNIIAYDHSRVILQPMEDDPSSdYINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIV 1016
Cdd:cd14599     37 ENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEW----HYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1017 MVTNLVEVGRVKCYKYWPD-----DAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHA 1091
Cdd:cd14599    112 MVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1092 TGLLSF------IRR--------VKMSNPptagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRIN 1157
Cdd:cd14599    192 QGFLSYleeiqsVRRhtnsmldsTKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMF 267

                          250
                   ....*....|....*..
gi 1207155729 1158 MVQTEEQYIFIHDAILE 1174
Cdd:cd14599    268 MIQTIAQYKFVYQVLIQ 284
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 917-1169 2.71e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 169.41  E-value: 2.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  917 EEYESFFEGQSASWDAAKKEQNRTKNRYGNIIAYDHSRVILQPmEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPV 996
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWID------GFEDDKKFIATQGPF 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  997 HETVYDFWRMIWQEQSACIVMVTNLVEV-GRVKCYKYW---PDDAEVYGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVR 1072
Cdd:PHA02747   103 AETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1073 EVKQFHFTGWPDHGVPYHATGLLSFI------RRVKMS--NPPTA--GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1142
Cdd:PHA02747   183 KISHFQCSEWFEDETPSDHPDFIKFIkiidinRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262

                          250       260
                   ....*....|....*....|....*..
gi 1207155729 1143 DIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:PHA02747   263 CLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1181-1476 6.21e-46

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: 167.60  E-value: 6.21e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1181 TAIPVCEFKAAYYDMIRIDSQSNSSHLKDEFQTLNSvtPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-E 1259
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLAS--SKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1260 SSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA--QGCPQYWPEEGMLRYGPV 1337
Cdd:cd14628     79 GSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWPAERSARYQYF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1338 QVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCL 1417
Cdd:cd14628    153 VVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPISVHCS 228

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1418 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1476
Cdd:cd14628    229 AGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 968-1170 2.06e-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: 162.96  E-value: 2.06e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVKCYKYWPDDAE-VYGDFKVT 1046
Cdd:cd14556      1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTLER--RGFNEVREVKQFHFTGWPDHG-VPYHATGLLSFIRRV-KMSNPPTAGPIVVHCSAGAGR 1122
Cdd:cd14556     74 FVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155729 1123 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14556    154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1181-1476 1.18e-44

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: 164.14  E-value: 1.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1181 TAIPVCEFKAAYYDMIRIDSQSNSSHLKDEFQTLnsVTPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-E 1259
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1260 SSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA--QGCPQYWPEEGMLRYGPV 1337
Cdd:cd14627     80 GSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMgrEKCHQYWPAERSARYQYF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1338 QVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCL 1417
Cdd:cd14627    154 VVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPISVHCS 229

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1418 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1476
Cdd:cd14627    230 AGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1229-1476 8.16e-44

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: 161.43  E-value: 8.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1229 ALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGC 1307
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNS 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1308 TSIVMLNEIDLA--QGCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAgHREVP 1385
Cdd:cd14629    122 TIVVMLTKLREMgrEKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTIRQFQFTDWP-EQGVP 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1386 ASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQY 1465
Cdd:cd14629    199 KTGEGFIDFIGQVHKTKEQFGQ-DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY 277

                          250
                   ....*....|.
gi 1207155729 1466 RFCYDLALEFI 1476
Cdd:cd14629    278 QLCYRAALEYL 288
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
941-1168 1.10e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 160.64  E-value: 1.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  941 KNRYGNIIAYDHSRVilqpMEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1020
Cdd:COG5599     45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1021 LVEVG--RVKCYKYWPDDAEvYGDFKV--TFVEVEPLAEYV-VRTFTLERRGFN-EVREVKQFHFTGWPDHGVPyHATGL 1094
Cdd:COG5599    111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1095 LSFIRRV----KMSNPPTaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1167
Cdd:COG5599    189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                   .
gi 1207155729 1168 I 1168
Cdd:COG5599    268 L 268
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 968-1169 2.60e-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: 2.60e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE-VGRVKCYKYWPDDA---EVYGDF 1043
Cdd:cd17658      1 YINASLVE----TPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEEnesREFGRI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1044 KVTFVEVEplaeyvVRTFTLERRGF----NEVRE----VKQFHFTGWPDHGVPYHATGLLSFIRRVKMSnPPTAGPIVVH 1115
Cdd:cd17658     77 SVTNKKLK------HSQHSITLRVLevqyIESEEpplsVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1116 CSAGAGRTGCYIVID-----IML-DMAeregVVDIYNCVKALRSRRINMVQTEEQYIFIH 1169
Cdd:cd17658    150 CSAGIGRTGAYCTIHntirrILEgDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1259-1474 2.99e-43

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: 157.51  E-value: 2.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1259 ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDL--AQGCPQYWPEEGMLRYGP 1336
Cdd:cd14623     22 ENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDcISCSMDCDVISRLFRICNLTRPQEGYlMVRQFQYLGWAgHREVPASKRSFLKLILQVDKWQEEceEGDGRTIIHC 1416
Cdd:cd14623     96 ITIE-LKKEEECESYTVRDLLVTNTRENKSR-QIRQFHFHGWP-EVGIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHC 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155729 1417 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14623    171 SAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 968-1170 3.52e-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: 3.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---AEVYGDFK 1044
Cdd:cd14539      1 YINASLIE-----DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAIT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1045 VTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---MSNPPTAGPIVVHCSAGAG 1121
Cdd:cd14539     76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1122 RTGCY-IVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1170
Cdd:cd14539    156 RTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 935-1172 1.55e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 155.96  E-value: 1.55e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  935 KEQNRTKNRYGNIIAYDHSRVILQPME-------------------DDPSSDYINANYIDiwlyrdGYQRPSHYIATQGP 995
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkievtsEDNAENYIHANFVD------GFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  996 VHETVYDFWRMIWQEQSACIVMVTNlVEVGRVKCYKYW--PDDAEV-YGDFKVTFVEVEPLAEYVVRTFTLERRGFNEVR 1072
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSR 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1073 EVKQFHFTGWPDHGVPYHATGLLSFIRRVKM----------SNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1142
Cdd:PHA02746   201 EIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV 280

                          250       260       270
                   ....*....|....*....|....*....|
gi 1207155729 1143 DIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:PHA02746   281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1073-1174 3.94e-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: 146.73  E-value: 3.94e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1073 EVKQFHFTGWPDHGVPYHATGLLSFIRRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1149
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1207155729  1150 ALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1073-1174 3.94e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 146.73  E-value: 3.94e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1073 EVKQFHFTGWPDHGVPYHATGLLSFIRRVK--MSNPPTAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1149
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1207155729  1150 ALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 968-1174 1.60e-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: 1.60e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-----DDAEVYGD 1042
Cdd:cd14598      1 YINASHIKVTVGGKEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1043 FKVTFVEVEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATGLLSF------IRRVKMSNPPTAG---PIV 1113
Cdd:cd14598     77 FKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRHTNSTIDPKSpnpPVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1114 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1199-1467 3.36e-40

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: 150.98  E-value: 3.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1199 DSQSNSSHLKDEFQTLNSVtpQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAA-LMDpseeyQ 1276
Cdd:cd14610     11 DHLKNKNRLEKEWEALCAY--QAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMD-----H 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1277 SYRQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI--DLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC-DVISR 1353
Cdd:cd14610     84 DPRNPA-YIATQGPLPATVADFWQMVWESGCVVIVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCeDFLVR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1354 LFRICNLTRPQEgyLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKwqeeCEEGDG-RTIIHCLNGGGRSGMFCAISIV 1432
Cdd:cd14610    163 SFYLKNLQTNET--RTVTQFHFLSWNDQG-VPASTRSLLDFRRKVNK----CYRGRScPIIVHCSDGAGRSGTYILIDMV 235

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207155729 1433 C-EMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14610    236 LnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1234-1474 3.25e-39

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: 146.39  E-value: 3.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVM 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 LNEIDLAQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCdviSRLFRICNL--TRPQEgylmVRQFQYLGWAGHrEVP 1385
Cdd:cd14553     77 MTKLEERSrvKCDQYWPTRGTETYGLIQVtllDTVELATYT---VRTFALHKNgsSEKRE----VRQFQFTAWPDH-GVP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1386 ASKRSFLKLILQVdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQY 1465
Cdd:cd14553    149 EHPTPFLAFLRRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQY 225


                   ....*....
gi 1207155729 1466 RFCYDLALE 1474
Cdd:cd14553    226 IFIHDALLE 234
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1239-1467 8.62e-39

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: 144.42  E-value: 8.62e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1239 RFMDNLPPDRCLPFLITIDGES-SNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEId 1317
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEgSDYINANYI------PGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQC- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1318 LAQG---CPQYWPE-EGMLRYGPVQVDCISCSMDCDVISRLFRICNltrpQEGYLMVRQFQYLGWAGHrEVPASKRSFLK 1393
Cdd:cd14548     74 MEKGrvkCDHYWPFdQDPVYYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1394 LILQVdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14548    149 FVRLV---RDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1263-1469 4.55e-38

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: 141.69  E-value: 4.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWPEEG-MLRYGPVQV-- 1339
Cdd:cd14550      1 YINASYL------QGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEkPLECETFKVtl 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 ---DCISCSMDCDVISRLFRICNltrPQEGY-LMVRQFQYLGWAghrEVPASKRSFLKLILQVDKWqeeCEEGDGRTIIH 1415
Cdd:cd14550     75 sgeDHSCLSNEIRLIVRDFILES---TQDDYvLEVRQFQCPSWP---NPCSPIHTVFELINTVQEW---AQQRDGPIVVH 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14550    146 DRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1228-1469 5.03e-38

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: 144.04  E-value: 5.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1228 IALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYG 1306
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMD------GYKQKNAYIATQGPLPKTYSDFWRMVWEQK 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1307 CTSIVMLNEIDlAQG---CPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRICNL----TRPqegylmVRQFQYLG 1377
Cdd:cd14543     97 VLVIVMTTRVV-ERGrvkCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTetdeSRQ------VTHFQFTS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1378 WAGHrEVPASKRSFLKLILQVDKWQEECEEGDGRT----------IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHA 1447
Cdd:cd14543    170 WPDF-GVPSSAAALLDFLGEVRQQQALAVKAMGDRwkghppgppiVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQT 248

                          250       260
                   ....*....|....*....|..
gi 1207155729 1448 VKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14543    249 VRRMRTQRAFSIQTPDQYYFCY 270
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1199-1467 1.03e-37

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: 143.64  E-value: 1.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1199 DSQSNSSHLKDEFQTLNSVtpQPQPEDCSIALLPRNHDKNRFMDNLPPDRC-LPFLITIDGESSNYINAALM---DPsee 1274
Cdd:cd14609      9 DHLRNRDRLAKEWQALCAY--QAEPNTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASPIiehDP--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1275 yqsyRQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI--DLAQGCPQYWPEEGMLRYGPVQVDCISCSMDC-DVI 1351
Cdd:cd14609     84 ----RMPA-YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCeDFL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1352 SRLFRICNLtRPQEGYLMVrQFQYLGWAGHrEVPASKRSFLKLILQVDKwqeeCEEGDGRTII-HCLNGGGRSGMFCAIS 1430
Cdd:cd14609    159 VRSFYLKNV-QTQETRTLT-QFHFLSWPAE-GIPSSTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGRTGTYILID 231

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1207155729 1431 IVC-EMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14609    232 MVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1263-1474 6.73e-35

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: 132.73  E-value: 6.73e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEGMLrYGPVQVD 1340
Cdd:cd14555      1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRvKCSRYWPDDTEV-YGDIKVT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1341 CISCSMDCDVISRLFricnlTRPQEGY---LMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCL 1417
Cdd:cd14555     74 LVETEPLAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV---KASNPPSAGPIVVHCS 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1418 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14555    145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1263-1469 7.76e-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: 132.57  E-value: 7.76e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALM---DPseeyqsyRQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML---NEIDLAQgCPQYWPEEGMLRYGP 1336
Cdd:cd14546      1 YINASTIydhDP-------RNPA-YIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDCISCSMDC-DVISRLFRICNL----TRpqegylMVRQFQYLGWAgHREVPASKRSFLKLILQVDKwqeeCEEGDGR 1411
Cdd:cd14546     72 YEVHLVSEHIWCdDYLVRSFYLKNLqtseTR------TVTQFHFLSWP-DEGIPASAKPLLEFRRKVNK----SYRGRSC 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1412 TII-HCLNGGGRSGMFCAISIVCE-MIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14546    141 PIVvHCSDGAGRTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1238-1467 4.41e-34

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: 130.98  E-value: 4.41e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1238 NRFMDNLPPDR---CLPflITIDGESSNYINAALM---DPSEeyqsyrqpAAFIVTQHPLPNTVKDFWRLVYDYGCTSIV 1311
Cdd:cd14547      1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINANYIrgyDGEE--------KAYIATQGPLPNTVADFWRMVWQEKTPIIV 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1312 MLNEIDLA-QGCPQYWPEEGMLRYGPVQVDCIScsmdcdVISRL-FRICNLT-RPQEGYLMVRQFQYLGWAGHrEVPASK 1388
Cdd:cd14547     71 MITNLTEAkEKCAQYWPEEENETYGDFEVTVQS------VKETDgYTVRKLTlKYGGEKRYLKHYWYTSWPDH-KTPEAA 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1389 RSFLKLILQVDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14547    144 QPLLSLVQEVEEARQT-EPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1234-1474 8.48e-34

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: 130.92  E-value: 8.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVM 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 L-NEIDLAQ-GCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFricnlTRPQEGY---LMVRQFQYLGWAGHrEVPAS 1387
Cdd:cd14630     77 VtNLVEVGRvKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTF-----TVQKKGYheiREIRQFHFTSWPDH-GVPCY 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1388 KRSFLKLILQVdKWQEECEEGDgrTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14630    150 ATGLLGFVRQV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226


                   ....*..
gi 1207155729 1468 CYDLALE 1474
Cdd:cd14630    227 VHDAILE 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1232-1469 1.21e-33

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 131.10  E-value: 1.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1232 PRNHDKNRFMDNLPPDR---CLPFLItiDGESSNYINAALMDPSEEYQSYrqpaafIVTQHPLPNTVKDFWRLVYDYGCT 1308
Cdd:cd14603     28 KENVKKNRYKDILPYDQtrvILSLLQ--EEGHSDYINANFIKGVDGSRAY------IATQGPLSHTVLDFWRMIWQYGVK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1309 SIVM-LNEIDLA-QGCPQYWP-EEGMLRYGPVQVDCISCS-MDCDVISRLFRI--CNLTRpqegylMVRQFQYLGWAGHr 1382
Cdd:cd14603    100 VILMaCREIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR------SVSHFQYMAWPDH- 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1383 EVPASKRSFLKLILQVDKWQeeceeGDGRT--IIHCLNGGGRSGMFCAISIVCEMIKRQNVVD---VFHAVKSLRNSKPN 1457
Cdd:cd14603    173 GIPDSPDCMLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPA 247

                          250
                   ....*....|..
gi 1207155729 1458 MVDSPEQYRFCY 1469
Cdd:cd14603    248 AVQTEEQYEFLY 259
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1238-1474 1.36e-33

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: 129.94  E-value: 1.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1238 NRFMDNLPPDRCLPFLITIDGESSNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEId 1317
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYM------PGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1318 LAQG---CPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGylMVRQFQYLGWAGHrEVPASKRSFLKL 1394
Cdd:cd14615     74 VEQGrtkCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESR--TVRHFHFTSWPDH-GVPETTDLLINF 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1395 ILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14615    151 RHLVREYMKQNPP-NSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1234-1474 1.58e-33

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: 131.31  E-value: 1.58e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYID------GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVM 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 LNEIDLAQ--GCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGH--REVPASK 1388
Cdd:cd14626    115 MTRLEEKSrvKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDHgvPEYPTPI 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1389 RSFLKLIlqvdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14626    193 LAFLRRV-------KACNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIF 265


                   ....*..
gi 1207155729 1468 CYDLALE 1474
Cdd:cd14626    266 IHEALLE 272
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1263-1469 3.88e-33

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: 127.54  E-value: 3.88e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEG--MLRYGPVQ 1338
Cdd:cd14542      1 YINANFI------KGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKkKCERYWPEEGeeQLQFGPFK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1339 VDCISCSMDCDVIsrLFRICNLTRPQEGYlMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQeecEEGDGRTIIHCLN 1418
Cdd:cd14542     75 ISLEKEKRVGPDF--LIRTLKVTFQKESR-TVYQFHYTAWPDH-GVPSSVDPILDLVRLVRDYQ---GSEDVPICVHCSA 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1419 GGGRSGMFCAISIVCEMIKRQNVVD---VFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14542    148 GCGRTGTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1263-1470 9.51e-33

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: 126.70  E-value: 9.51e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEGMLRYGPVQV 1339
Cdd:cd14549      1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNL-VERGrrkCDQYWPKEGTETYGNIQV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 DCISCSMDCDVISRLFRICNL----TRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQeecEEGDGRTIIH 1415
Cdd:cd14549     74 TLLSTEVLATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAAN---PPGAGPIVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14549    150 CSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1257-1474 1.05e-32

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: 127.06  E-value: 1.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1257 DGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQ-GCPQYWPEEGMLrY 1334
Cdd:cd14631      9 DDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRvKCYKYWPDDTEV-Y 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1335 GPVQVDCISCSMDCDVISRLFricnlTRPQEGYLMVR---QFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGR 1411
Cdd:cd14631     82 GDFKVTCVEMEPLAEYVVRTF-----TLERRGYNEIRevkQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGP 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1412 TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14631    153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 968-1174 2.79e-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: 2.79e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDAE-VYGDFKVT 1046
Cdd:cd14634      1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTL--ERRGFNEVREVKQFHFTGWPDH-GVPYHATGLLSFIRRVKMSNPP---TAGPIVVHCSAGA 1120
Cdd:cd14634     73 FVSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1121 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14634    153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1238-1473 2.86e-32

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: 126.21  E-value: 2.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1238 NRFMDNLPPDRCLPFLITIDGES-SNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeI 1316
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFI------PGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-V 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1317 DLAQG---CPQYWPEEGM-LRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGYlmVRQFQYLGWAGHR--EVPASKRS 1390
Cdd:cd14618     74 GMENGrvlCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDHGipESTSSLMA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1391 FLKLILQvdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14618    152 FRELVRE----HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                   ...
gi 1207155729 1471 LAL 1473
Cdd:cd14618    228 CIL 230
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1263-1470 4.10e-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: 125.05  E-value: 4.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDPSEEYQSYrqpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EIDLAQG-CPQYWPEEGM-LRYGPVQV 1339
Cdd:cd18533      1 YINASYITLPGTSSKR-----YIATQGPLPATIGDFWKMIWQNNVGVIVMLTpLVENGREkCDQYWPSGEYeGEYGDLTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 DCISCSM--DCDVISRLFRicnLTRPQEGYLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCL 1417
Cdd:cd18533     76 ELVSEEEndDGGFIVREFE---LSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELNDSASL-DPPIIVHCS 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1418 NGGGRSGMFCAISIVCEMIKRQNVVD---------VFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd18533    151 AGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1234-1478 4.14e-32

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: 126.42  E-value: 4.14e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLITIDGE--SSNYINAALMDPSEEYQSYRQPA-AFIVTQHPLPNTVKDFWRLVYDYGCTSI 1310
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINANYIRNENEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1311 VMLNEiDLAQG---CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFricNLTRPQEGYLM--VRQFQYLGWAGHrEV 1384
Cdd:cd14544     81 VMTTK-EVERGknkCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIreIWHYQYLSWPDH-GV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDS 1461
Cdd:cd14544    156 PSDPGGVLNFLEDVNQRQESLPHA-GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQT 234

                          250
                   ....*....|....*..
gi 1207155729 1462 PEQYRFCYDLALEFIET 1478
Cdd:cd14544    235 EAQYKFIYVAVAQYIET 251
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1231-1476 6.25e-32

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: 126.75  E-value: 6.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1231 LPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTS 1309
Cdd:cd14625     44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSAT 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1310 IVMLNEIDLAQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCDVISRLFRICNLTRPQegylmVRQFQYLGWAGHrEV 1384
Cdd:cd14625    118 VVMMTKLEEKSriKCDQYWPSRGTETYGMIQVtllDTIELATFCVRTFSLHKNGSSEKRE-----VRQFQFTAWPDH-GV 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSFLKLILQVdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPE 1463
Cdd:cd14625    192 PEYPTPFLAFLRRV----KTCNPPDaGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTED 267

                          250
                   ....*....|...
gi 1207155729 1464 QYRFCYDLALEFI 1476
Cdd:cd14625    268 QYSFIHDALLEAV 280
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1244-1474 8.11e-32

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: 124.67  E-value: 8.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1244 LPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQ 1320
Cdd:cd14620      5 LPYDHSRVILSQLDGiPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1321 GCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRI----CNLTRPQEgylMVRQFQYLGWA--GHREVPASKRSFLKL 1394
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIqpqlPDGCKAPR---LVTQLHFTSWPdfGVPFTPIGMLKFLKK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1395 ILQVDKWQEeceegdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14620    156 VKSVNPVHA------GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1234-1474 1.38e-31

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: 125.54  E-value: 1.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLITIDGES-SNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:cd14633     40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYID------GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 L-NEIDLAQ-GCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFRIcnLTRPQEGYLMVRQFQYLGWAGHrEVPASKRS 1390
Cdd:cd14633    114 VtNLVEVGRvKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATG 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1391 FLKLILQVdkwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14633    190 LLGFVRQV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                   ....
gi 1207155729 1471 LALE 1474
Cdd:cd14633    267 AILE 270
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1234-1478 1.58e-31

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: 124.74  E-value: 1.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLpfLITIDGE----SSNYINAALMDPSEEYQSY--RQPAAFIVTQHPLPNTVKDFWRLVYDYGC 1307
Cdd:cd14605      2 NKNKNRYKNILPFDHTR--VVLHDGDpnepVSDYINANIIMPEFETKCNnsKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1308 TSIVMLN-EIDLAQG-CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFRicnLTRPQEGYL--MVRQFQYLGWAGHr 1382
Cdd:cd14605     80 RVIVMTTkEVERGKSkCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELK---LSKVGQGNTerTVWQYHFRTWPDH- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1383 EVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMV 1459
Cdd:cd14605    156 GVPSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                          250
                   ....*....|....*....
gi 1207155729 1460 DSPEQYRFCYDLALEFIET 1478
Cdd:cd14605    235 QTEAQYRFIYMAVQHYIET 253
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1236-1469 4.79e-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: 122.50  E-value: 4.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1236 DKNRFMDNLPPDRCLpflITIDGESSNYINAALMDPSEEYQSYrqpaafIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE 1315
Cdd:cd14545      2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSY------ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1316 I--DLAQGCPQYWP----EEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGHrEVPASKR 1389
Cdd:cd14545     73 LmeKGQIKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1390 SFLKLILQVdKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV--VDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14545    150 AFLNFLQKV-RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228


                   ..
gi 1207155729 1468 CY 1469
Cdd:cd14545    229 SY 230
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1284-1467 5.70e-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: 5.70e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1284 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEG-MLRYGPVQVDCISCSMDCDVISRLFRICN 1359
Cdd:cd14541     21 YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTL-VERGrvkCHQYWPDLGeTMQFGNLQITCVSEEVTPSFAFREFILTN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1360 LTRPQEGYlmVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEgdgRTIIHCLNGGGRSGMFCAISIVCEMIKRQ 1439
Cdd:cd14541    100 TNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE---PTVVHCSAGIGRTGVLITMETAMCLIEAN 173

                          170       180
                   ....*....|....*....|....*...
gi 1207155729 1440 NVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14541    174 EPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 968-1168 6.15e-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: 121.27  E-value: 6.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCykYWPDDAEV--YGDFKV 1045
Cdd:cd14550      1 YINASYLQ------GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVE-----VEPLAEYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATglLSFIRRVKMSNPPTAGPIVVHCSAGA 1120
Cdd:cd14550     73 TLSGedhscLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGG 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1207155729 1121 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFI 1168
Cdd:cd14550    151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1238-1476 8.77e-31

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: 121.92  E-value: 8.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1238 NRFMDNLPPDRCLPFLITIDGE-SSNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI 1316
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYM------PGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1317 DLAQ--GCPQYWPeegmLRYGPVQVDCISCSMDCDVISRLFRICNLT---RPQEGYLMVRQFQYLGWAGHrEVPASKRSF 1391
Cdd:cd14619     75 MEAGrvKCEHYWP----LDYTPCTYGHLRVTVVSEEVMENWTVREFLlkqVEEQKTLSVRHFHFTAWPDH-GVPSSTDTL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1392 LKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1471
Cdd:cd14619    150 LAFRRLLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                   ....*
gi 1207155729 1472 ALEFI 1476
Cdd:cd14619    229 ILDFL 233
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1237-1474 9.14e-31

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: 121.87  E-value: 9.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1237 KNRFMDNLPPDRCLP--FLITIDgESSNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-L 1313
Cdd:cd14602      1 KNRYKDILPYDHSRVelSLITSD-EDSDYINANFI------KGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1314 NEIDLA-QGCPQYWPEEG--MLRYGPVQVDCISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGWAGHrEVPASKRS 1390
Cdd:cd14602     74 MEFEMGkKKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1391 FLKLILQVDKWQEEceegDGRTI-IHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDSPEQYR 1466
Cdd:cd14602    149 ILELIWDVRCYQED----DSVPIcIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYE 224


                   ....*...
gi 1207155729 1467 FCYDLALE 1474
Cdd:cd14602    225 LVYNAVIE 232
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1263-1474 2.15e-30

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: 119.77  E-value: 2.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-IDLAQ-GCPQYWPEEGMLrYGPVQVD 1340
Cdd:cd14632      1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlVEVGRvKCSKYWPDDSDT-YGDIKIT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1341 CISCSMDCDVISRLFricnlTRPQEGYLM---VRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIHCL 1417
Cdd:cd14632     74 LLKTETLAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVVHCS 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1418 NGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14632    145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1231-1476 2.69e-30

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: 122.15  E-value: 2.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1231 LPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTS 1309
Cdd:cd14624     44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSAT 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1310 IVMLNEIDLAQ--GCPQYWPEEGMLRYGPVQV---DCISCSMDCDVISRLFRICNLTRPQegylmVRQFQYLGWAGHrEV 1384
Cdd:cd14624    118 VVMMTKLEERSrvKCDQYWPSRGTETYGLIQVtllDTVELATYCVRTFALYKNGSSEKRE-----VRQFQFTAWPDH-GV 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSFLKLILQVdkwqEECEEGD-GRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPE 1463
Cdd:cd14624    192 PEHPTPFLAFLRRV----KTCNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTED 267

                          250
                   ....*....|...
gi 1207155729 1464 QYRFCYDLALEFI 1476
Cdd:cd14624    268 QYIFIHDALLEAV 280
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1234-1465 3.94e-30

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: 121.96  E-value: 3.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRC-LPFLITIDGESSNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:cd14604     57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFI------KGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 -LNEIDLA-QGCPQYWPE--EGMLRYGPVQVDCISCSMDCDVISR--LFRICNLTRpqegylMVRQFQYLGWAGHrEVPA 1386
Cdd:cd14604    131 aCREFEMGrKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRtlLLEFQNETR------RLYQFHYVNWPDH-DVPS 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1387 SKRSFLKLILQVDKWQeecEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNMVDSPE 1463
Cdd:cd14604    204 SFDSILDMISLMRKYQ---EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKE 280


                   ..
gi 1207155729 1464 QY 1465
Cdd:cd14604    281 QY 282
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 968-1174 4.46e-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: 4.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMvtnLVEVGRVK-CYKYWPDDAEV-YGDFKV 1045
Cdd:cd14636      1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQgCPQYWPEEGMLrYGPIQV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLAEYVVRTF-----TLERRGFNEVRevkQFHFTGWPDH-GVPYHATGLLSFIRRVKMSNPPT---AGPIVVHC 1116
Cdd:cd14636     72 ECMSCSMDCDVISRIFricnlTRPQEGYLMVQ---QFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECdegEGRTIIHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155729 1117 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14636    149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1223-1467 6.01e-30

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: 120.35  E-value: 6.01e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1223 PEDCSIALLPRnhdKNRFMDNLPPDRCLPFLITIDGES--SNYINAALMdpseeyQSY-RQPAAFIVTQHPLPNTVKDFW 1299
Cdd:cd14613     17 PKEYDIPGLVR---KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYI------RGYgGEEKVYIATQGPTVNTVGDFW 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1300 RLVYDYGCTSIVMLNEID-LAQGCPQYWPEEGMLrYGPVQVDCISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGW 1378
Cdd:cd14613     88 RMVWQERSPIIVMITNIEeMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSW 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1379 AGHReVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNM 1458
Cdd:cd14613    163 PDQK-TPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGM 241


                   ....*....
gi 1207155729 1459 VDSPEQYRF 1467
Cdd:cd14613    242 IQTCEQYQF 250
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1369-1474 1.27e-29

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 113.99  E-value: 1.27e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1369 MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMI-KRQNVVDVFHA 1447
Cdd:smart00404    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 1207155729  1448 VKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1369-1474 1.27e-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: 113.99  E-value: 1.27e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  1369 MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMI-KRQNVVDVFHA 1447
Cdd:smart00012    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 1207155729  1448 VKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1223-1473 1.90e-29

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: 118.40  E-value: 1.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1223 PEDCSIallPRNHDKNRFMDNLP-PDR--CLPFLITIDgESSNYINAALMdpseeyQSYR-QPAAFIVTQHPLPNTVKDF 1298
Cdd:cd14612      7 PEELDI---PGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYI------RGYDgKEKAYIATQGPMLNTVSDF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1299 WRLVYDYGCTSIVMLNEI-DLAQGCPQYWPE-EGmlRYGPVQVDcISCSMDCDVisrlFRICNLT-RPQEGYLMVRQFQY 1375
Cdd:cd14612     77 WEMVWQEECPIIVMITKLkEKKEKCVHYWPEkEG--TYGRFEIR-VQDMKECDG----YTIRDLTiQLEEESRSVKHYWF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1376 LGWAGHrEVPASKRSFLKLILQVDKwQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSK 1455
Cdd:cd14612    150 SSWPDH-QTPESAGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDR 227

                          250
                   ....*....|....*....
gi 1207155729 1456 PNMVDSPEQYRFCY-DLAL 1473
Cdd:cd14612    228 GGMIQTSEQYQFLHhTLAL 246
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1237-1469 2.47e-29

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: 117.33  E-value: 2.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1237 KNRFMDNLPPDRCLPFLIT--IDGESSNYINAALMdpseeyQSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML 1313
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYI------RGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1314 NEI-DLAQGCPQYWPEEGMLrYGPVQVdCISCSMDCDvisrLFRICNLTRPQEGYLM-VRQFQYLGWAGHReVPASKRSF 1391
Cdd:cd14611     76 TKLkEKNEKCVLYWPEKRGI-YGKVEV-LVNSVKECD----NYTIRNLTLKQGSQSRsVKHYWYTSWPDHK-TPDSAQPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155729 1392 LKLILQVDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14611    149 LQLMLDVEEDRLA-SPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1229-1467 3.60e-29

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: 117.68  E-value: 3.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1229 ALLPRNHDKNRFMDNLPPDRCLPFLITI-DGESSNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGC 1307
Cdd:cd14614      7 ADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYI------PGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1308 TSIVMLNEIDLAQ--GCPQYWP-EEGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEgylmVRQFQYLGWAGHrEV 1384
Cdd:cd14614     81 QIIVMLTQCNEKRrvKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDH-GV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSflKLILQ-VDKWQEECEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPE 1463
Cdd:cd14614    156 PTANAA--ESILQfVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 233


                   ....
gi 1207155729 1464 QYRF 1467
Cdd:cd14614    234 QYIF 237
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1263-1469 5.82e-29

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: 115.78  E-value: 5.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEID--LAQGCPQYWPEEGMLRYGPVQVD 1340
Cdd:cd14551      1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKerKEKKCSQYWPDQGCWTYGNLRVR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1341 CISCSMDCDVISRLF------RICNLTRPQegylMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTII 1414
Cdd:cd14551     75 VEDTVVLVDYTTRKFciqkvnRGIGEKRVR----LVTQFHFTSWPDF-GVPFTPIGMLKFLKKV---KSANPPRAGPIVV 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1415 HCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14551    147 HCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1226-1477 7.15e-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: 117.82  E-value: 7.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1226 CSIALLPRNHDKNRFMDNLPPDRCLpflITIDGESSNYINAALMDPSEEYQSYrqpaafIVTQHPLPNTVKDFWRLVYDY 1305
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSY------ILTQGPLPNTCGHFWEMVWEQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1306 GCTSIVMLNEIdLAQG---CPQYWPE----EGMLRYGPVQVDCISCSMDCDVISRLFRICNLTRPQEGYLMvrQFQYLGW 1378
Cdd:cd14608     88 KSRGVVMLNRV-MEKGslkCAQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL--HFHYTTW 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1379 AGHrEVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFC-AISIVCEMIKRQN--VVDVFHAVKSLRNSK 1455
Cdd:cd14608    165 PDF-GVPESPASFLNFLFKVRESGSLSPE-HGPVVVHCSAGIGRSGTFClADTCLLLMDKRKDpsSVDIKKVLLEMRKFR 242

                          250       260
                   ....*....|....*....|..
gi 1207155729 1456 PNMVDSPEQYRFCYdlaLEFIE 1477
Cdd:cd14608    243 MGLIQTADQLRFSY---LAVIE 261
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 968-1174 7.69e-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: 7.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDA-EVYGDFKVT 1046
Cdd:cd14635      1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENGvHRHGPIQVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1047 FVEVEPLAEYVVRTFTL--ERRGFNEVREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KMSNPPTAGPIVVHCSAGA 1120
Cdd:cd14635     73 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1121 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1207-1474 1.63e-28

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: 117.43  E-value: 1.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1207 LKDEFqtlNSVTPQPQPEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDG-ESSNYINAALMDpseeyqSYRQPAAFI 1285
Cdd:cd14621     28 FREEF---NALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFIN------GYQEKNKFI 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1286 VTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQ--GCPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICNL--- 1360
Cdd:cd14621     99 AAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdv 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1361 --TRPQEgylMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEegdGRTIIHCLNGGGRSGMFCAISIVCEMIKR 1438
Cdd:cd14621    179 tnKKPQR---LITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHA 251

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1207155729 1439 QNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14621    252 ERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1238-1469 5.61e-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: 113.48  E-value: 5.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1238 NRFMDNLPPDRCLPFLITIDGES-SNYINAALMdPSEEYQSyrqpaAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI 1316
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYI-PGNNFRR-----EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1317 dLAQG---CPQYWP-EEGMLRYGPVQVDCISCSMDCDVISRLFRICN---LTRPQegylMVRQFQYLGWAGHrEVPASKR 1389
Cdd:cd14617     75 -VEKGrvkCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSeeqLDAPR----LVRHFHYTVWPDH-GVPETTQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1390 SFLKLILQVDKWQEEcEEGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd14617    149 SLIQFVRTVRDYINR-TPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 968-1174 2.80e-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: 2.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINAnyidiwLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDDA-EVYGDFKV 1045
Cdd:cd14637      1 YINA------ALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGlQQYGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLAEYVVRTFTLER--RGFNEVREVKQFHFTGW-PDHGVPYHATGLLSFIRRV-KMSNPPTAGPIVVHCSAGAG 1121
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1122 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1174
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1232-1478 6.15e-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: 111.90  E-value: 6.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1232 PRNHDKNRFMDNLPPDRCLPFLITIDGE-------SSNYINAALMDPSEeyqsyrQPAAFIVTQHPLPNTVKDFWRLVYD 1304
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDE------NAKTYIASQGCLEATVNDFWQMAWQ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1305 YGCTSIVMLN-EIDLAQG-CPQYWPEEGMLR-YGPVQVDCISCSMDCDVISRLFRICNLTRpQEGYLMVRQFQYLGWAGH 1381
Cdd:cd14606     90 ENSRVIVMTTrEVEKGRNkCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1382 rEVPASKRSFLKLILQVDKWQEECEEGdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKSLRNSKPNM 1458
Cdd:cd14606    169 -GVPSEPGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGM 246

                          250       260
                   ....*....|....*....|
gi 1207155729 1459 VDSPEQYRFCYDLALEFIET 1478
Cdd:cd14606    247 VQTEAQYKFIYVAIAQFIET 266
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1263-1470 8.98e-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: 109.40  E-value: 8.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMdpsEEYQSYRQPaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLA-QGCPQYWPEE--GMLRYGPVQ 1338
Cdd:cd14539      1 YINASLI---EDLTPYCPR--FIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEkQKVHRYWPTErgQALVYGAIT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1339 VDCISCSMDCDVISRLFRICNltRPQEGYLMVRQFQYLGWAGHReVPASKRSFLKLILQVDKWQEECEEGDGRTIIHCLN 1418
Cdd:cd14539     76 VSLQSVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1419 GGGRSGMFC-AISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd14539    153 GVGRTGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 968-1173 1.62e-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: 1.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYkYWPDDAE--VYGDFKV 1045
Cdd:cd17669      1 YINASYIM------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFKV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLA-----EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHATglLSFIRRVKMSNPPTAGPIVVHCSAGA 1120
Cdd:cd17669     74 TLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1121 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1173
Cdd:cd17669    152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1263-1473 2.31e-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: 108.16  E-value: 2.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEI-DLAQGCPQYWPEEGMlrygPVQVDC 1341
Cdd:cd17669      1 YINASYI------MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDE----PINCET 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1342 ISCSM---DCDVISR----LFRICNLTRPQEGYLM-VRQFQYLGWAgHREVPASKRSFLKLILqvdkwQEECEEGDGRTI 1413
Cdd:cd17669     71 FKVTLiaeEHKCLSNeeklIIQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKTFELISII-----KEEAANRDGPMI 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1414 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1473
Cdd:cd17669    145 VHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1261-1467 3.90e-26

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: 108.07  E-value: 3.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1261 SNYINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEG--MLRYG 1335
Cdd:cd14616     25 SDYINASYI------SGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC-FEKGrirCHQYWPEDNkpVTVFG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1336 PVQVDCISCSMDCDVISRLFRIcnltRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIH 1415
Cdd:cd14616     98 DIVITKLMEDVQIDWTIRDLKI----ERHGDYMMVRQCNFTSWPEH-GVPESSAPLIHFVKLV---RASRAHDNTPMIVH 169

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRF 1467
Cdd:cd14616    170 CSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1263-1474 5.28e-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: 5.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDPSEEYQSYRqpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeIDLAQG---CPQYWPE---EGMLRYGP 1336
Cdd:cd14538      1 YINASHIRIPVGGDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVT-QDVEGGkvkCHRYWPDslnKPLICGGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDCISCSMDCDVISRLFricNLTRPQEGYL-MVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWqeeceEGDGRTIIH 1415
Cdd:cd14538     76 LEVSLEKYQSLQDFVIRRI---SLRDKETGEVhHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRI-----HNSGPIVVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14538    147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1263-1473 5.33e-26

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: 107.07  E-value: 5.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMdpseeyQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEIDLAQGCPQYWP--EEGM----LRYG 1335
Cdd:cd17670      1 YINASYI------MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPsrEESMnceaFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1336 PVQVDCISCSMDCDVISRLFRicnLTRPQEGYLM-VRQFQYLGWAGHREVPASKRSFLKLIlqvdkwQEECEEGDGRTII 1414
Cdd:cd17670     75 LISKDRLCLSNEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIV 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1415 HCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLAL 1473
Cdd:cd17670    146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1263-1476 6.49e-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: 107.54  E-value: 6.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDPSEEYQSYRqpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML--NEIDLAQGCPQYWP----EEGMLRYGP 1336
Cdd:cd14540      1 YINASHITATVGGKQRF----YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPtlggEHDALTFGE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDC-ISCSMDCDVISRLfRICNLTRPQegYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEEC-EEGDGR--- 1411
Cdd:cd14540     77 YKVSTkFSVSSGCYTTTGL-RVKHTLSGQ--SRTVWHLQYTDWPDH-GCPEDVSGFLDFLEEINSVRRHTnQDVAGHnrn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1412 --TIIHCLNGGGRSG--MFCAISIVCemIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFI 1476
Cdd:cd14540    153 ppTLVHCSAGVGRTGvvILADLMLYC--LDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1227-1467 9.58e-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: 108.40  E-value: 9.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1227 SIALLPRNHDKNRFMDNLPPDRCLPFLitidGESSNYINAALMDpsEEYQSYRQPAAFIVTQHPLPNTVKDFWRLVYDYG 1306
Cdd:cd14600     33 TCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVN--MEIPSANIVNKYIATQGPLPHTCAQFWQVVWEQK 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1307 CTSIVMLNEIDlAQG---CPQYWPE-EGMLRYGPVQVDCisCSMDCDvISRLFRICNLTRPQEG-YLMVRQFQYLGWAGH 1381
Cdd:cd14600    107 LSLIVMLTTLT-ERGrtkCHQYWPDpPDVMEYGGFRVQC--HSEDCT-IAYVFREMLLTNTQTGeERTVTHLQYVAWPDH 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1382 rEVPASKRSFLKLILQVDKWQEECEEgdgrTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDS 1461
Cdd:cd14600    183 -GVPDDSSDFLEFVNYVRSKRVENEP----VLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQT 257


                   ....*.
gi 1207155729 1462 PEQYRF 1467
Cdd:cd14600    258 SSQYKF 263
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1232-1476 2.49e-25

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: 107.43  E-value: 2.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1232 PRNHDKNRFMDNLPPDRC---LPFLITIDGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCT 1308
Cdd:cd17667     25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVD------GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1309 SIVMLNEIdLAQG---CPQYWPEEGMLRYGPVQVDCISCSMDCDVISRLFRICN--LTRPQEG-------YLMVRQFQYL 1376
Cdd:cd17667     99 IIVMITNL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYT 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1377 GWAgHREVPASKRSFLKLILQVDKWQEEceeGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKP 1456
Cdd:cd17667    178 QWP-DMGVPEYALPVLTFVRRSSAARTP---EMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRN 253

                          250       260
                   ....*....|....*....|
gi 1207155729 1457 NMVDSPEQYRFCYDLALEFI 1476
Cdd:cd17667    254 YLVQTEEQYIFIHDALLEAI 273
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1263-1469 4.90e-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: 104.47  E-value: 4.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALM-DPSEEYQSyrqpaAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQG---CPQYWP-EEGMLR-YGP 1336
Cdd:cd17658      1 YINASLVeTPASESLP-----KFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaEENESReFGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDCISCSMDCDVISRLFRICNLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLIlqvdKWQEECEEGDGRTIIHC 1416
Cdd:cd17658     76 ISVTNKKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSVRELL----KRLYGIPPSAGPIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207155729 1417 LNGGGRSGMFCAISIVCEMIKRQNV--VDVFHAVKSLRNSKPNMVDSPEQYRFCY 1469
Cdd:cd17658    151 SAGIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1223-1475 8.21e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 106.62  E-value: 8.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1223 PEDCSIALLPRNHDKNRFMDNLPPDRCLPFLITIDGeSSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLV 1302
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVD------GHNAKGRFICTQAPLEETALDFWQAI 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1303 YDYGCTSIVMLNEI--DLAQGCPQYW--PEEGMLRYGPVQVDCISCSMdcdviSRLFRICNL--TRPQEG-YLMVRQFQY 1375
Cdd:PHA02742   114 FQDQVRVIVMITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAY 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1376 LGWAgHREVPASKRSFLKLILQVDKWQEECE---EGDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHA 1447
Cdd:PHA02742   189 EDWP-HGGLPRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                          250       260
                   ....*....|....*....|....*...
gi 1207155729 1448 VKSLRNSKPNMVDSPEQYRFCYDLALEF 1475
Cdd:PHA02742   268 VRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 968-1173 1.30e-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: 1.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  968 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDAEVYG--DFKV 1045
Cdd:cd17670      1 YINASYIM------GYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSREESMNceAFTV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1046 TFVEVEPLA-----EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGVPYHAT-GLLSFIRRVKMSNPptaGPIVVHCSAG 1119
Cdd:cd17670     74 TLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRD---GPTIVHDEFG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1120 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1173
Cdd:cd17670    151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1228-1469 3.61e-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: 103.51  E-value: 3.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1228 IALLPRNHDKNRFMDNLPPDRCLpflITIDGESSNYINAALMDPSEEYQSYrqpaafIVTQHPLPNTVKDFWRLVYDYGC 1307
Cdd:cd14607     18 VAKYPENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSY------ILTQGPLPNTCCHFWLMVWQQKT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1308 TSIVMLNEI--DLAQGCPQYWP--EEGMLRYGPV--QVDCISCSMDCDVISRLFRICNLTRPQEgyLMVRQFQYLGWAGH 1381
Cdd:cd14607     89 KAVVMLNRIveKDSVKCAQYWPtdEEEVLSFKETgfSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1382 rEVPASKRSFLKLILQVDKWQEECEEgDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQN--VVDVFHAVKSLRNSKPNMV 1459
Cdd:cd14607    167 -GVPESPASFLNFLFKVRESGSLSPE-HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244

                          250
                   ....*....|
gi 1207155729 1460 DSPEQYRFCY 1469
Cdd:cd14607    245 QTPDQLRFSY 254
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1260-1477 5.92e-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: 101.56  E-value: 5.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1260 SSNYINAALMDPSEEYQsyrqpaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNeIDLAQG---CPQYWPE-EGMLRYG 1335
Cdd:cd14601      4 NANYINMEIPSSSIINR-------YIACQGPLPNTCSDFWQMTWEQGSSMVVMLT-TQVERGrvkCHQYWPEpSGSSSYG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1336 PVQVDCISCSMDCDVISRLFRICNLTRPQEGYLMvrQFQYLGWAGHrEVPASKRSFLKLILQVdkwQEECEEGDGRTIIH 1415
Cdd:cd14601     76 GFQVTCHSEEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1416 CLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1477
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1263-1465 2.95e-23

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: 99.13  E-value: 2.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQ--GCPQYWP--EEGMLRYGPVQ 1338
Cdd:cd14557      1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNrnKCAQYWPsmEEGSRAFGDVV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1339 VDCISCSMDCDVISRLFRICNlTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEEceeGDGRTIIHCLN 1418
Cdd:cd14557     75 VKINEEKICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFNNF---FSGPIVVHCSA 149

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207155729 1419 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQY 1465
Cdd:cd14557    150 GVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1222-1467 4.15e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 102.00  E-value: 4.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1222 QPEDCSIA--LLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAALMDPSEEyqsyrqPAAFIVTQHPLPNTVKDFW 1299
Cdd:PHA02747    37 KPFDGLIAnfEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFED------DKKFIATQGPFAETCADFW 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1300 RLVYDYGCTSIVMLNEIDLAQG---CPQYW--PEEGMLRYGPVQVDCISCSMDCDVISRLFRICNltRPQEGYLMVRQFQ 1374
Cdd:PHA02747   111 KAVWQEHCSIIVMLTPTKGTNGeekCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1375 YLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGDGR-------TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHA 1447
Cdd:PHA02747   189 CSEWFED-ETPSDHPDFIKFIKIIDINRKKSGKLFNPkdallcpIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKT 267

                          250       260
                   ....*....|....*....|
gi 1207155729 1448 VKSLRNSKPNMVDSPEQYRF 1467
Cdd:PHA02747   268 AEKIREQRHAGIMNFDDYLF 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1263-1470 4.83e-23

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: 98.90  E-value: 4.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIdLAQG---CPQYWPEEGMLRYGPVQV 1339
Cdd:cd17668      1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPADGSEEYGNFLV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1340 DCISCSMDCDVISRLFRICNLT--------RPQEgyLMVRQFQYLGWAgHREVPASKrsfLKLILQVDKWQEECEEGDGR 1411
Cdd:cd17668     74 TQKSVQVLAYYTVRNFTLRNTKikkgsqkgRPSG--RVVTQYHYTQWP-DMGVPEYT---LPVLTFVRKASYAKRHAVGP 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1412 TIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYD 1470
Cdd:cd17668    148 VVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1263-1474 1.81e-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: 94.04  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1263 YINAA--LMDPSEEYQSYrqpaafIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN-EIDLAQ-GCPQYWPE--EGMLRYGP 1336
Cdd:cd14596      1 YINASyiTMPVGEEELFY------IATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKvKCHRYWPEtlQEPMELEN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1337 VQVDCISCSMDCDVISRLFRICNltRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEEceegdGRTIIHC 1416
Cdd:cd14596     75 YQLRLENYQALQYFIIRIIKLVE--KETGENRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHC 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207155729 1417 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALE 1474
Cdd:cd14596    147 SAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1254-1476 1.25e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 94.71  E-value: 1.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1254 ITIDGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLA-QGCPQYW--PEEG 1330
Cdd:PHA02746    91 VTSEDNAENYIHANFVD------GFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDdEKCFELWtkEEDS 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1331 MLRYGPVQVDCISCSMDCDVISRLFRICNLTrpQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECE---- 1406
Cdd:PHA02746   165 ELAFGRFVAKILDIIEELSFTKTRLMITDKI--SDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAELIkqad 241

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207155729 1407 ---EGDGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYdLALEFI 1476
Cdd:PHA02746   242 ndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKYA 313
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1234-1473 6.62e-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: 90.27  E-value: 6.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1234 NHDKNRFMDNLPPDRCLPFLitidGESSNYINAALMD---PSEEYqsyrqpaAFIVTQHPLPNTVKDFWRLVYDYGCTSI 1310
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKmpvGDEEF-------VYIACQGPLPTTVADFWQMVWEQKSTVI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1311 VML-NEIDLAQ-GCPQYWPEEgmLRyGPVQVD---CISCSMDCDVISRLFRICNLTRPQEGYL-MVRQFQYLGWAGHrEV 1384
Cdd:cd14597     72 AMMtQEVEGGKiKCQRYWPEI--LG-KTTMVDnrlQLTLVRMQQLKNFVIRVLELEDIQTREVrHITHLNFTAWPDH-DT 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1385 PASKRSFLKLILQVDKWQEEceegdGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQ 1464
Cdd:cd14597    148 PSQPEQLLTFISYMRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQ 222


                   ....*....
gi 1207155729 1465 YRFCYDLAL 1473
Cdd:cd14597    223 YIFCYQVIL 231
PHA02738 PHA02738
hypothetical protein; Provisional
 1233-1479 7.42e-19

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 89.60  E-value: 7.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1233 RNHDKNRFMDNLPPDRCLPFLITiDGESSNYINAALMDpseeyqSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM 1312
Cdd:PHA02738    48 KNRKLNRYLDAVCFDHSRVILPA-ERNRGDYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1313 L--NEIDLAQGCPQYWP--EEGMLRYGPVQVDCISCSMDCDVISRLFRicnLTRPQEGYLMVRQFQYLGWAGHrEVPASK 1388
Cdd:PHA02738   121 LckKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLL---LTDGTSATQTVTHFNFTAWPDH-DVPKNT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1389 RSFLKLILQVDKWQEECEE-----GDGRT-----IIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKSLRNSKPNM 1458
Cdd:PHA02738   197 SEFLNFVLEVRQCQKELAQeslqiGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYS 276

                          250       260
                   ....*....|....*....|.
gi 1207155729 1459 VDSPEQYRFCYDLALEFIETS 1479
Cdd:PHA02738   277 LFIPFQYFFCYRAVKRYVNLT 297
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1219-1477 5.74e-18

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: 86.20  E-value: 5.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1219 PQPQPEDC-SIALLPRNHDKNRFMDNLPPDRCLPFLITIDGESSNYINAA---LMDPSEEYQsyrqpaaFIVTQHPLPNT 1294
Cdd:cd14599     22 PKKKADGVfTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINAShikVTVGGEEWH-------YIATQGPLPHT 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1295 VKDFWRLVYDYGCTSIVMLNEiDLAQGCPQ---YWPEEGMLR----YGPVQVDC-ISCSMDCDVISRLfRICNLTRPQEG 1366
Cdd:cd14599     95 CHDFWQMVWEQGVNVIAMVTA-EEEGGRSKshrYWPKLGSKHssatYGKFKVTTkFRTDSGCYATTGL-KVKHLLSGQER 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1367 ylMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKWQEECEEGDGRT-------IIHCLNGGGRSGMFCAISIVCEMIKRQ 1439
Cdd:cd14599    173 --TVWHLQYTDWPDH-GCPEEVQGFLSYLEEIQSVRRHTNSMLDSTkncnppiVVHCSAGVGRTGVVILTELMIGCLEHN 249

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1207155729 1440 NVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1477
Cdd:cd14599    250 EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 895-1172 2.23e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.77  E-value: 2.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  895 IRVADLLQHInlmkTSDSYGFKEEYESffEGQSASWDAAKKEQNrtKNRYGNIIAYDHSRVILQPMEDDPSSDYInanyi 974
Cdd:PHA02740    18 INKPDLLSCI----IKEYRAIVPEHED--EANKACAQAENKAKD--ENLALHITRLLHRRIKLFNDEKVLDARFV----- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  975 diwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVgrvKCY-KYWPDD---AEVYGDFKVTFVEV 1050
Cdd:PHA02740    85 ------DGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKegcVITSDKFQIETLEI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1051 EPLAEYVVRTFTLERRgFNEVREVKQFHFTGWPDHGVPYHATGLLSFIRRV--------KMSNPPTAGPIVVHCSAGAGR 1122
Cdd:PHA02740   156 IIKPHFNLTLLSLTDK-FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGISS 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1123 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1172
Cdd:PHA02740   235 SAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
fn3 pfam00041
Fibronectin type III domain;
491-582 6.65e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 68.60  E-value: 6.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  491 PVPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVPllrppllVSLPWNTSRYNFTLLHPGTTYQFLI 570
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNE-------ITVPGTTTSVTLTGLKPGTEYEVRV 73

                           90
                   ....*....|..
gi 1207155729  571 RASTSKGFGPPT 582
Cdd:pfam00041   74 QAVNGGGEGPPS 85
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1284-1477 8.28e-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: 8.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1284 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN--EIDLAQGCPQYWPEEG----MLRYGPVQVDC-ISCSMDCDVISRLfR 1356
Cdd:cd14598     18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPRLGsrhnTVTYGRFKITTrFRTDSGCYATTGL-K 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1357 ICNLTRPQEgyLMVRQFQYLGWA--GHREVPASKRSFLKLILQVDKWQEECEEGDGRT---IIHCLNGGGRSGMFCAISI 1431
Cdd:cd14598     97 IKHLLTGQE--RTVWHLQYTDWPehGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNppvLVHCSAGVGRTGVVILSEI 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207155729 1432 VCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLALEFIE 1477
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 2.76e-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: 2.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGIITQYEISYSSVHSFDPSVpllrpplLVSLPWNTSRYNFTLLHPGTTYQF 568
Cdd:cd00063      1 PSP-PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE-------VEVTPGSETSYTLTGLKPGTEYEF 72

                           90       100
                   ....*....|....*....|.
gi 1207155729  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) ...
 969-1165 1.16e-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: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  969 INANYIDIwlyrdGYQRPShyIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDaEVYGDFKVTFV 1048
Cdd:cd14559     18 LNANRVQI-----GNKNVA--IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQS-GTYGSVTVKSK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1049 EVEPLA---EYVVRTFTLERRGFNEVREVKQFHFTGWPDHGvPYHATGLLSFIRRVKMS----------------NPPTA 1109
Cdd:cd14559     90 KTGKDElvdGLKADMYNLKITDGNKTITIPVVHVTNWPDHT-AISSEGLKELADLVNKSaeekrnfykskgssaiNDKNK 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207155729 1110 GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIyncVKALR-SRRINMVQTEEQY 1165
Cdd:cd14559    169 LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRtSRNGKMVQKDEQL 222
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1077-1170 1.56e-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: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1077 FHFTGWPDHGVPyhATGLLSFIRRVKMSNPPTAGPIVVHCSAGAGRTG----CYIVidIMLDMAEREgvvdiynCVKALR 1152
Cdd:cd14506     79 FYNFGWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLV--YALRMSADQ-------AIRLVR 147

                           90
                   ....*....|....*...
gi 1207155729 1153 SRRINMVQTEEQYIFIHD 1170
Cdd:cd14506    148 SKRPNSIQTRGQVLCVRE 165
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 489-579 9.33e-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: 9.33e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   489 PGPvPKEFVRSTPSEDKISLQWKEPLEPNGI--ITQYEISYSSVHSfdpsvpllrPPLLVSLPWNTSRYNFTLLHPGTTY 566
Cdd:smart00060    1 PSP-PSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGS---------EWKEVNVTPSSTSYTLTGLKPGTEY 70

                            90
                    ....*....|...
gi 1207155729   567 QFLIRASTSKGFG 579
Cdd:smart00060   71 EFRVRAVNGAGEG 83
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1278-1471 2.43e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.20  E-value: 2.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1278 YRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEIDLAQGCPQYWP--EEGMLRYGPVQVDCIscsmdcDVISR-- 1353
Cdd:PHA02740    87 YDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSlkEGCVITSDKFQIETL------EIIIKph 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1354 -LFRICNLTRPQEGYLMVRQFQYLGWAGHrEVPASKRSFLKLILQVDKW--QEECEEGDGRT---IIHCLNGGGRSGMFC 1427
Cdd:PHA02740   161 fNLTLLSLTDKFGQAQKISHFQYTAWPAD-GFSHDPDAFIDFFCNIDDLcaDLEKHKADGKIapiIIDCIDGISSSAVFC 239

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207155729 1428 AISIVCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPEQYRFCYDL 1471
Cdd:PHA02740   240 VFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHL 283
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 201-282 4.25e-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: 4.25e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   201 GDVEVNAGQNATFQCiaTVRDAVNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQSERGSGVS 280
Cdd:smart00410    2 PSVTVKEGESVTLSC--EASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79


                    ..
gi 1207155729   281 NF 282
Cdd:smart00410   80 GT 81
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1384-1470 1.02e-06

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: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1384 VPASKRSFLKLIlqvdKWQEECEEGDGRTIIHCLNGGGRSGMFCAisivCEMIKRQNVVDVFHAVKSLRNSKPNMVDSPE 1463
Cdd:cd14505     85 VPSDIAQWQELL----EELLSALENGKKVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156


                   ....*..
gi 1207155729 1464 QYRFCYD 1470
Cdd:cd14505    157 QENFLHQ 163
fn3 pfam00041
Fibronectin type III domain;
293-370 2.06e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  293 PIAPPQLLGVGPTYLLIQLNANSiFGDGPIILKEVEYRMTSGSWTETHAVNSPN---YKLWHLDPDTEYEIRVlLTRPGE 369
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEITVPGTttsVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 1207155729  370 G 370
Cdd:pfam00041   80 G 80
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1110-1170 4.22e-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: 4.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729 1110 GPIVVHCSAGAGRTGCYIVIDIMLDMaeREGVVDIYNCVKALRSRRINmvQTEEQYIFIHD 1170
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGGIP--QTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1082-1170 1.20e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1082 WPDHGVPyHATGLLSFIRRVKMSNPPTaGPIVVHCSAGAGRTG----CYIVidimldmaeREGvVDIYNCVKALRSRRIN 1157
Cdd:COG2453     55 IPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGtvaaAYLV---------LLG-LSAEEALARVRAARPG 122

                           90
                   ....*....|...
gi 1207155729 1158 MVQTEEQYIFIHD 1170
Cdd:COG2453    123 AVETPAQRAFLER 135
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
452-631 2.51e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 48.85  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  452 VVGNLPPNTNVSLKMILTNPEGRKESDETLIQTQEDVPGPVPKEFVRSTPSEDKISLQWKEPLEPNgiITQYEISYSSVH 531
Cdd:COG3401    195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD--ATGYRVYRSNSG 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  532 SFDPSVpllrpplLVSLpwNTSRYNFTLLHPGTTYQFLIRASTSKGF--GPPTTLNVTTNISAPTleeydgseASLNETA 609
Cdd:COG3401    273 DGPFTK-------VATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPA--------APSGLTA 335

                          170       180
                   ....*....|....*....|....*
gi 1207155729  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 3.67e-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: 3.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729   291 PRPIAPPQLLGVGPTYLLIQ-LNANSIFGDGPIILKEVEYRMTSGSWTETHA-VNSPNYKLWHLDPDTEYEIRVL-LTRP 367
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVtPSSTSYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 1207155729   368 GEG 370
Cdd:smart00060   81 GEG 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1403-1470 4.01e-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: 4.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207155729 1403 EECEEGDGRTIIHCLNGGGRSGMFCAisivCEMIKRQNvVDVFHAVKSLRNSKPN-MVDSPEQYRFCYD 1470
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 5.36e-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: 5.36e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207155729  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 6.41e-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: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  291 PRPIAPPQLLGVGPTYLLIQLNANSifGDGPIILK-EVEYR-MTSGSWTE--THAVNSPNYKLWHLDPDTEYEIRVLLTR 366
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....*..
gi 1207155729  367 pgEGGTGQPGPALITRT 383
Cdd:cd00063     79 --GGGESPPSESVTVTT 93
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1112-1170 3.44e-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: 3.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207155729 1112 IVVHCSAGAGRTG----CYIvidIMLDM-AEREGVVDIyncVKALRSRRInmvQTEEQYIFIHD 1170
Cdd:cd14505    109 VLIHCKGGLGRTGliaaCLL---LELGDtLDPEQAIAA---VRALRPGAI---QTPKQENFLHQ 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1111-1168 8.07e-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: 8.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207155729 1111 PIVVHCSAGAGRTG----CYIVIDIMLDMAEregvvdiynCVKALRSRRINMVQTEEQYIFI 1168
Cdd:cd14504     84 AVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
I-set pfam07679
Immunoglobulin I-set domain;
195-277 1.00e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  195 PHFLR-LGDVEVNAGQNATFQCIAT------VRdavnnklWLqrRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLY 267
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTgtpdpeVS-------WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKY 71

                           90
                   ....*....|
gi 1207155729  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 1.92e-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: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729  193 KSPHflrlgDVEVNAGQNATFQCIATVRDavNNKLWLQRRNGEDIPVAEKKNINHRKFAASFRLKEVSSQDQDLYRCVTQ 272
Cdd:cd05763      4 KTPH-----DITIRAGSTARLECAATGHP--TPQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQ 76

                           90
                   ....*....|....*
gi 1207155729  273 SERGSGVSNfAGLIV 287
Cdd:cd05763     77 NSAGSISAN-ATLTV 90
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1356-1472 7.75e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.41  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207155729 1356 RICNLTRPQEGYLMVR-----QFQYLGWAGHRevPASKRSFLKLILQVDKWQEEceegDGRTIIHCLNGGGRSGMFCAis 1430
Cdd:COG2453     28 AVVSLTEEEELLLGLLeeaglEYLHLPIPDFG--APDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA-- 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1207155729 1431 ivCEMIKRQnvVDVFHAVKSLRNSKPNMVDSPEQYRFCYDLA 1472
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.
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