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Conserved domains on  [gi|634743231|ref|NP_001278910|]
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receptor-type tyrosine-protein phosphatase kappa isoform c precursor [Homo sapiens]

Protein Classification

MAM and R-PTPc-K-2 domain-containing protein( domain architecture ID 13891800)

protein containing domains MAM, IG_like, FN3, and R-PTPc-K-2

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 ...
 888-1166 2.05e-160

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: 484.16  E-value: 2.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  888 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwl 967
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  968 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVV 1047
Cdd:cd14633    78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1048 RTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1127
Cdd:cd14633   155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 634743231 1128 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1252-1457 5.41e-151

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: 456.41  E-value: 5.41e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC 1331
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1332 DVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:cd14636    81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1412 IGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14636   161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 32-192 2.28e-58

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: 198.34  E-value: 2.28e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231     32 SAGGCTFDDGPgACDYHQDLYDDFEWVHVSAQEP---HYLPPEMPQGSYMIVDSSDHDPGEKARLQLPTMKEN-DTHCID 107
Cdd:smart00137    2 SPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    108 FSYLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTfWPNEYQVIFEAEVSGGRSGYIAIDDIQV 187
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 634743231    188 LSYPC 192
Cdd:smart00137  157 SNGPC 161
fn3 pfam00041
Fibronectin type III domain;
488-583 3.95e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   488 DVPGPVPVKSLQGTSfenkIFLNWKEPLDPNGIITQYEISYSSIRSFDpavpvagPPQTVSNLWNSTHHVFMHLHPGTTY 567
Cdd:pfam00041    1 SAPSNLTVTDVTSTS----LTVSWTPPPDGNGPITGYEVEYRPKNSGE-------PWNEITVPGTTTSVTLTGLKPGTEY 69

                           90
                   ....*....|....*.
gi 634743231   568 QFFIRASTVKGFGPAT 583
Cdd:pfam00041   70 EVRVQAVNGGGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 202-288 5.45e-08

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: 51.74  E-value: 5.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    202 GDVEVNAGQNATFQCIATGRDAVHnkLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSgVS 281
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPE--VTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS-AS 78


                    ....*..
gi 634743231    282 NFAQLIV 288
Cdd:smart00410   79 SGTTLTV 85
fn3 pfam00041
Fibronectin type III domain;
294-371 6.26e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   294 PIAPPQLLGVGPTYLLIQLNANSIiGDGPIILKEVEYRMTSGSWTETHAV---NAPTYKLWHLDPDTEYEIRVlLTRPGE 370
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 634743231   371 G 371
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 ...
 888-1166 2.05e-160

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: 484.16  E-value: 2.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  888 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwl 967
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  968 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVV 1047
Cdd:cd14633    78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1048 RTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1127
Cdd:cd14633   155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 634743231 1128 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1252-1457 5.41e-151

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: 456.41  E-value: 5.41e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC 1331
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1332 DVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:cd14636    81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1412 IGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14636   161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
903-1163 6.04e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 372.76  E-value: 6.04e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    903 GFKEEYESFFEGQSA--SWDVAKKDQNRAKNRYGNIIAYDHSRVILQPvEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 980
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    981 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGY 1057
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1058 NEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1137
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 634743231   1138 KALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
927-1163 3.02e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 364.26  E-value: 3.02e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   927 NRAKNRYGNIIAYDHSRVILQPVEDDpsSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1007 VTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEP-LAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATG 1082
Cdd:pfam00102   73 LTELEEKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1083 LLSFIRRV-KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 634743231  1162 LE 1163
Cdd:pfam00102  233 LE 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1223-1457 2.62e-84

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 275.27  E-value: 2.62e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1223 NHDKNRFMDMLPPDRCLPFLiTIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVD-- 1300
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1301 LSQGCPQYWPE--EGMLRYGPIQVECMSCSMDC-DVINRIFRICNLTRPQEgyLMVQQFQYLGWaSHREVPGSKRSFLKL 1377
Cdd:pfam00102   80 GREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGW-PDHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1378 ILQVEKWQEECEEGegRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:pfam00102  157 LRKVRKSSLDGRSG--PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1196-1457 1.75e-82

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 271.45  E-value: 1.75e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1196 LKDEFQTLNSVTPrlQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLP 1275
Cdd:smart00194    2 LEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1276 NTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPEEG--MLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyL 1351
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLtELVEKGReKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET--R 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1352 MVQQFQYLGWaSHREVPGSKRSFLKLILQVEKWQeecEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAV 1431
Cdd:smart00194  158 TVTHYHYTNW-PDHGVPESPESILDLIRAVRKSQ---STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 634743231   1432 KTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 32-192 2.28e-58

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: 198.34  E-value: 2.28e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231     32 SAGGCTFDDGPgACDYHQDLYDDFEWVHVSAQEP---HYLPPEMPQGSYMIVDSSDHDPGEKARLQLPTMKEN-DTHCID 107
Cdd:smart00137    2 SPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    108 FSYLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTfWPNEYQVIFEAEVSGGRSGYIAIDDIQV 187
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 634743231    188 LSYPC 192
Cdd:smart00137  157 SNGPC 161
PHA02738 PHA02738
hypothetical protein; Provisional
 881-1161 4.30e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 197.84  E-value: 4.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  881 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDVAKKdqNRAKNRYGNIIAYDHSRVILqPVEDDpSS 955
Cdd:PHA02738    6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD---DTEVYGDF 1032
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveqGSIRFGKF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1033 KVTCVEMEPLAEYVVRTFTLErRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------LSNPP 1096
Cdd:PHA02738  150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1097 sagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:PHA02738  229 ---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 36-192 1.08e-51

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: 179.10  E-value: 1.08e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    36 CTFDDGPgACDYHQDLYDDFEWVHVSAQEPHYLPPE-----MPQGSYMIVDSSDHDPGEKARLQLPTMKENDT-HCIDFS 109
Cdd:pfam00629    1 CDFEDGN-LCGWTQDSSDDFDWERVSGPSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   110 YLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFwPNEYQVIFEAEVSGGRSGYIAIDDIQVLS 189
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 634743231   190 YPC 192
Cdd:pfam00629  156 GPC 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 36-192 2.86e-51

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: 177.96  E-value: 2.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   36 CTFDDGpgACDYHQDLYDDFEWVHVSAQEPHYLPP-----EMPQGSYMIVDSSDHDPGEKARLQLPTMKEN-DTHCIDFS 109
Cdd:cd06263     1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  110 YLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWpNEYQVIFEAEVSGGRSGYIAIDDIQVLS 189
Cdd:cd06263    79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 634743231  190 YPC 192
Cdd:cd06263   155 GPC 157
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
930-1157 4.42e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 4.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVilqpVEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1009
Cdd:COG5599    45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1010 LVEVG--RVKCYKYWPDDTEvYGDFKV--TCVEMEPLAEYV-VRTFTLERRGYN-EIREVKQFHFTGWPDHGVPyHATGL 1083
Cdd:COG5599   111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1084 LSFIRRV----KLSNPPSaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1156
Cdd:COG5599   189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                  .
gi 634743231 1157 I 1157
Cdd:COG5599   268 L 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1215-1458 1.08e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 115.10  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1215 CSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGeSSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIV 1294
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1295 MLNEV--DLSQGCPQYW--PEEGMLRYGPIQVECMSCSMdcdviNRIFRICNL--TRPQEG-YLMVQQFQYLGWAsHREV 1367
Cdd:PHA02742  123 MITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAYEDWP-HGGL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1368 PGSKRSFLKLILQVEKWQEECE---EGEGRT-----IIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKP 1439
Cdd:PHA02742  197 PRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRH 276

                         250
                  ....*....|....*....
gi 634743231 1440 NMVEAPEQYRFCYDVALEY 1458
Cdd:PHA02742  277 NCLSLPQQYIFCYFIVLIF 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1189-1461 7.20e-25

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 106.33  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1189 SQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPR------NHDKNRFMDMLPPDRclpfliTIDGESSNYINAA---LMD 1259
Cdd:COG5599     2 SPKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQylqninGSPLNRFRDIQPYKE------TALRANLGYLNANyiqVIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1260 SYRqpaaFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLS---QGCPQYWPEEGmlRYGpiQVECMSCSMDCDVIN 1335
Cdd:COG5599    76 NHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLaSDDEISkpkVKMPVYFRQDG--EYG--KYEVSSELTESIQLR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1336 R--IFRICNLTRPQEG--YLMVQQFQYLGWASHRevPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:COG5599   148 DgiEARTYVLTIKGTGqkKIEIPVLHVKNWPDHG--AISAEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIA 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1412 IGIVVEMVKRQNV--VDVFHAVKTLRNSK-PNMVEAPEQyrfcYDVALEYLES 1461
Cdd:COG5599   226 CLALSKSINALVQitLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
fn3 pfam00041
Fibronectin type III domain;
488-583 3.95e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   488 DVPGPVPVKSLQGTSfenkIFLNWKEPLDPNGIITQYEISYSSIRSFDpavpvagPPQTVSNLWNSTHHVFMHLHPGTTY 567
Cdd:pfam00041    1 SAPSNLTVTDVTSTS----LTVSWTPPPDGNGPITGYEVEYRPKNSGE-------PWNEITVPGTTTSVTLTGLKPGTEY 69

                           90
                   ....*....|....*.
gi 634743231   568 QFFIRASTVKGFGPAT 583
Cdd:pfam00041   70 EVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 488-589 1.28e-11

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: 62.13  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  488 DVPGPVPVKSLQGTSfenkIFLNWKEPLDPNGIITQYEISYSSIRSfdpavpvaGPPQTV-SNLWNSTHHVFMHLHPGTT 566
Cdd:cd00063     2 SPPTNLRVTDVTSTS----VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVeVTPGSETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 634743231  567 YQFFIRASTVKGFG-PATAINVTT 589
Cdd:cd00063    70 YEFRVRAVNGGGESpPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 492-580 2.97e-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: 52.23  E-value: 2.97e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    492 PVPVKSLQGTSF-ENKIFLNWKEPLDPNGI--ITQYEISYSsirsfdpavPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQ 568
Cdd:smart00060    1 PSPPSNLRVTDVtSTSVTLSWEPPPDDGITgyIVGYRVEYR---------EEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71

                            90
                    ....*....|..
gi 634743231    569 FFIRASTVKGFG 580
Cdd:smart00060   72 FRVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 202-288 5.45e-08

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: 51.74  E-value: 5.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    202 GDVEVNAGQNATFQCIATGRDAVHnkLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSgVS 281
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPE--VTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS-AS 78


                    ....*..
gi 634743231    282 NFAQLIV 288
Cdd:smart00410   79 SGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
459-632 5.42e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.16  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  459 PYTNVSLKMILTNPEGRKESEETIIQTDEDVPgPVPVKSLQGTS-FENKIFLNWKEPLDPNgiITQYEISYSSIRSfdpa 537
Cdd:COG3401   201 PGTTYYYRVAATDTGGESAPSNEVSVTTPTTP-PSAPTGLTATAdTPGSVTLSWDPVTESD--ATGYRVYRSNSGD---- 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  538 vpvaGPPQTVSNLwNSTHHVFMHLHPGTTYQFFIRASTVKGF--GPATAINVTTNISAPTLPdyEGVDASlNETATTITv 615
Cdd:COG3401   274 ----GPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPAAP--SGLTAT-AVGSSSIT- 344

                         170
                  ....*....|....*..
gi 634743231  616 lLRPAQAKGAPISAYQI 632
Cdd:COG3401   345 -LSWTASSDADVTGYNV 360
fn3 pfam00041
Fibronectin type III domain;
294-371 6.26e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   294 PIAPPQLLGVGPTYLLIQLNANSIiGDGPIILKEVEYRMTSGSWTETHAV---NAPTYKLWHLDPDTEYEIRVlLTRPGE 370
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 634743231   371 G 371
Cdd:pfam00041   80 G 80
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 206-276 1.52e-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: 44.83  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231  206 VNAGQNATFQCIATGrDAVHNKLWlqRRNGEDIPVAQTKNINHRrfaASFRLQEVTKTDQDLYRCVTQSER 276
Cdd:cd20957    13 VDFGRTAVFNCSVTG-NPIHTVLW--MKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYQCFVRNDG 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 292-371 3.10e-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: 3.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    292 PRPIAPPQLLGVGPTYLLIQ-LNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPT-YKLWHLDPDTEYEIRVL-LTRP 368
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 634743231    369 GEG 371
Cdd:smart00060   81 GEG 83
I-set pfam07679
Immunoglobulin I-set domain;
196-288 3.30e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.79  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   196 PHFLR-LGDVEVNAGQNATFQCIATGR---DAVhnklWLqrRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCV 271
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTGTpdpEVS----WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74

                           90
                   ....*....|....*..
gi 634743231   272 TQSERGSgVSNFAQLIV 288
Cdd:pfam07679   75 ATNSAGE-AEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 292-384 4.86e-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: 43.64  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  292 PRPIAPPQLLGVGPTYLLIQLNANSiiGDGPIILK-EVEYR-MTSGSWTE--THAVNAPTYKLWHLDPDTEYEIRVLLTR 367
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....*..
gi 634743231  368 pgEGGTGLPGPPLITRT 384
Cdd:cd00063    79 --GGGESPPSESVTVTT 93
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 888-1166 2.05e-160

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: 484.16  E-value: 2.05e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  888 DLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwl 967
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYID--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  968 yrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVV 1047
Cdd:cd14633    78 ---GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1048 RTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAER 1127
Cdd:cd14633   155 RTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 234

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 634743231 1128 EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd14633   235 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 943-1166 1.24e-157

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 474.51  E-value: 1.24e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  943 RVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 1022
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYID------GYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1023 PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 1102
Cdd:cd14631    75 PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1103 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd14631   155 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1252-1457 5.41e-151

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: 456.41  E-value: 5.41e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC 1331
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1332 DVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:cd14636    81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1412 IGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14636   161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 957-1166 1.61e-147

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: 447.06  E-value: 1.61e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTC 1036
Cdd:cd14555     1 YINANYID------GYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1037 VEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYI 1116
Cdd:cd14555    75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 634743231 1117 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd14555   155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 925-1167 9.87e-140

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: 427.90  E-value: 9.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  925 DQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 1004
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYID------GYHRPRHYIATQGPMQETVKDFWRMIWQENSASV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1005 VMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLL 1084
Cdd:cd14630    75 VMVTNLVEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1085 SFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1164
Cdd:cd14630   155 GFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234


                  ...
gi 634743231 1165 CLC 1167
Cdd:cd14630   235 CLC 237
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 957-1167 5.32e-127

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


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 392.11  E-value: 5.32e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTC 1036
Cdd:cd14632     1 YINANYID------GYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1037 VEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYI 1116
Cdd:cd14632    75 LKTETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1117 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1167
Cdd:cd14632   155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 925-1167 7.25e-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: 393.30  E-value: 7.25e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  925 DQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACI 1004
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCD------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1005 VMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGL 1083
Cdd:cd14553    75 VMMTKLEERSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1084 LSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14553   155 LAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234


                  ....
gi 634743231 1164 ACLC 1167
Cdd:cd14553   235 AVTC 238
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1252-1453 8.21e-124

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: 383.30  E-value: 8.21e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLS-QGCPQYWPEEGMLRYGPIQVECMSCSMD 1330
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKdQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1331 CDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECeeGEGRTIIHCLNGGGRSGMFC 1410
Cdd:cd14556    81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 634743231 1411 AIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
903-1163 6.04e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 372.76  E-value: 6.04e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    903 GFKEEYESFFEGQSA--SWDVAKKDQNRAKNRYGNIIAYDHSRVILQPvEDDPSSDYINANYIDiwlyrdGYQRPSHYIA 980
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYID------GPNGPKAYIA 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    981 TQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGY 1057
Cdd:smart00194   74 TQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1058 NEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCV 1137
Cdd:smart00194  154 SETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 634743231   1138 KALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
927-1163 3.02e-116

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 364.26  E-value: 3.02e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   927 NRAKNRYGNIIAYDHSRVILQPVEDDpsSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYID------GYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVM 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1007 VTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEP-LAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATG 1082
Cdd:pfam00102   73 LTELEEKGREKCAQYWPeeeGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1083 LLSFIRRV-KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:pfam00102  153 LLDLLRKVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232


                   ..
gi 634743231  1162 LE 1163
Cdd:pfam00102  233 LE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 887-1167 4.18e-112

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 354.73  E-value: 4.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  887 ADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiw 966
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYID-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  967 lyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVEMEPLAEY 1045
Cdd:cd14626    79 ----GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1046 VVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1125
Cdd:cd14626   155 SVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 634743231 1126 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1167
Cdd:cd14626   235 KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1252-1457 8.79e-111

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 348.16  E-value: 8.79e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC 1331
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1332 DVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:cd14634    81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1412 IGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14634   161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 881-1167 1.71e-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: 1.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  881 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINA 960
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  961 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DTEVYGDFKVTCVEM 1039
Cdd:cd14625    81 NYID------GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSrGTETYGMIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1040 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVID 1119
Cdd:cd14625   155 IELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVID 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1120 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLC 1167
Cdd:cd14625   235 AMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 881-1168 6.89e-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: 6.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  881 HPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINA 960
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  961 NYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DTEVYGDFKVTCVEM 1039
Cdd:cd14624    81 NYID------GYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSrGTETYGLIQVTLLDT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1040 EPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVID 1119
Cdd:cd14624   155 VELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVID 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1120 IMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCG 1168
Cdd:cd14624   235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1252-1457 4.06e-105

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: 332.81  E-value: 4.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC 1331
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1332 DVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:cd14635    81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1412 IGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14635   161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1252-1457 9.92e-104

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 328.79  E-value: 9.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQG---CPQYWPEEGMLRYGPIQVECMSCS 1328
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSawpCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1329 MDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECeeGEGRTIIHCLNGGGRSGM 1408
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRES--GEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1409 FCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 957-1159 5.59e-99

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: 315.38  E-value: 5.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE---VYGDFK 1033
Cdd:cd00047     1 YINASYID------GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG 1113
Cdd:cd00047    75 VTLVSEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1114 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd00047   155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 957-1159 4.33e-93

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: 298.88  E-value: 4.33e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKVT 1035
Cdd:cd14549     1 YINANYVD------GYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTL------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGA 1109
Cdd:cd14549    75 LLSTEVLATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd14549   155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 932-1158 6.88e-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: 293.49  E-value: 6.88e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  932 RYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 1011
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIP------GYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1012 EVGRVKCYKYWPDDTE--VYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSFIRR 1089
Cdd:cd14548    75 EKGRVKCDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 634743231 1090 VKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14548   153 VRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 877-1172 1.36e-85

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: 281.53  E-value: 1.36e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  877 TGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQ-SASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSS 955
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKV 1034
Cdd:cd14621    81 DYINASFIN------GYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgCWTYGNIRV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLAEYVVRTFTLERRG----YNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAG 1110
Cdd:cd14621   155 SVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVG 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 634743231 1111 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAI 1172
Cdd:cd14621   235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 904-1166 7.24e-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: 278.84  E-value: 7.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  904 FKEEYEsffEGQSASWDV------AKKDQNRAKNRYGNIIAYDHSRVILQPV--EDDPSSDYINANYIDiwlyrdGYQRP 975
Cdd:cd17667     1 FSEDFE---EVQRCTADMnitaehSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVD------GYNKA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  976 SHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVTCVEMEPLAEYVVRTFTLER 1054
Cdd:cd17667    72 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1055 -----------RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLD 1123
Cdd:cd17667   152 tkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQ 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 634743231 1124 MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 1166
Cdd:cd17667   232 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1223-1457 2.62e-84

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 275.27  E-value: 2.62e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1223 NHDKNRFMDMLPPDRCLPFLiTIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVD-- 1300
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEek 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1301 LSQGCPQYWPE--EGMLRYGPIQVECMSCSMDC-DVINRIFRICNLTRPQEgyLMVQQFQYLGWaSHREVPGSKRSFLKL 1377
Cdd:pfam00102   80 GREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEET--RTVKHFHYTGW-PDHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  1378 ILQVEKWQEECEEGegRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:pfam00102  157 LRKVRKSSLDGRSG--PIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1196-1457 1.75e-82

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 271.45  E-value: 1.75e-82
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1196 LKDEFQTLNSVTPrlQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLP 1275
Cdd:smart00194    2 LEEEFEKLDRLKP--DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1276 NTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPEEG--MLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyL 1351
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLtELVEKGReKCAQYWPDEEgePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET--R 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1352 MVQQFQYLGWaSHREVPGSKRSFLKLILQVEKWQeecEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAV 1431
Cdd:smart00194  158 TVTHYHYTNW-PDHGVPESPESILDLIRAVRKSQ---STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*.
gi 634743231   1432 KTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 927-1161 1.01e-81

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: 268.95  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDD-PSSDYINANYIDIWLYRDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACI 1004
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIRNENEGPTTDENAKtYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1005 VMVTNLVEVGRVKCYKYWPDD--TEVYGDFKVTCVEMEPLAEYVVRTFTLERRG-YNEIREVKQFHFTGWPDHGVPYHAT 1081
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1082 GLLSFIRRV--KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIF 1156
Cdd:cd14544   161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ....*
gi 634743231 1157 IHDAI 1161
Cdd:cd14544   241 IYVAV 245
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 903-1158 9.79e-81

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: 266.92  E-value: 9.79e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  903 GFKEEYESF-FEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIAT 981
Cdd:cd14543     4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMD------GYKQKNAYIAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  982 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYN 1058
Cdd:cd14543    78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1059 EIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------------LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMA 1125
Cdd:cd14543   158 ESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqalavkamgdrWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237

                         250       260       270
                  ....*....|....*....|....*....|...
gi 634743231 1126 EREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14543   238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 933-1163 2.19e-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: 261.41  E-value: 2.19e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  933 YGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE 1012
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYID------GYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1013 VGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEI---REVKQFHFTGWPDHGVPYHATGLLSFIR 1088
Cdd:cd14620    75 RKEEKCYQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLK 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1089 RVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14620   155 KVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 931-1158 1.73e-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: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1009
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIR------GYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1010 LVEvGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSFIR 1088
Cdd:cd14547    75 LTE-AKEKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQ 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 634743231 1089 RVK--LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14547   152 EVEeaRQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 931-1163 4.82e-77

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: 254.81  E-value: 4.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1010
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMP------GYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1011 VEVGRVKCYKYWPDDTE--VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIR 1088
Cdd:cd14619    75 MEAGRVKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 634743231 1089 RVK--LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14619   155 LLRqwLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 931-1163 1.25e-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: 250.50  E-value: 1.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQpVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1010
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMP------GYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1011 VEVGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--I 1087
Cdd:cd14615    74 VEQGRTKCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1088 RRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14615   154 VREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 927-1162 1.84e-75

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: 250.52  E-value: 1.84e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFID------GYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEVGRVKCYKYWPDDTEV-YGDFKVtcvemEPLAE-----YVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHA 1080
Cdd:cd14554    80 LTKLREMGREKCHQYWPAERSArYQYFVV-----DPMAEynmpqYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1081 TGLLSFIRRVKLSNPP--SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14554   155 EGFIDFIGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                  ....
gi 634743231 1159 DAIL 1162
Cdd:cd14554   235 RAAL 238
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 957-1162 3.18e-73

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: 242.96  E-value: 3.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFKVT 1035
Cdd:cd17668     1 YINANYVD------GYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTLE--------RRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSA 1107
Cdd:cd17668    75 QKSVQVLAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1108 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1162
Cdd:cd17668   155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 957-1158 6.15e-72

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: 239.04  E-value: 6.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE-VYGDFKVT 1035
Cdd:cd14551     1 YINASYID------GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTLER--RGYNE--IREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGR 1111
Cdd:cd14551    75 VEDTVVLVDYTTRKFCIQKvnRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 634743231 1112 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14551   155 TGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 926-1161 8.57e-72

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: 240.69  E-value: 8.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  926 QNRAKNRYGNIIAYDHSRVILQPVE-DDPSSDYINANYI--DIWLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSA 1002
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImpEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1003 CIVMVTNLVEVGRVKCYKYWPDDTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGY-NEIREVKQFHFTGWPDHGVPYH 1079
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1080 ATGLLSFIRRVKLSNP--PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQY 1154
Cdd:cd14605   161 PGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                  ....*..
gi 634743231 1155 IFIHDAI 1161
Cdd:cd14605   241 RFIYMAV 247
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 957-1159 2.25e-71

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: 237.53  E-value: 2.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDIwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DTEVYGDFKV 1034
Cdd:cd18533     1 YINASYITL-----PGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgeYEGEYGDLTV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEME--PLAEYVVRTFTLeRRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV--KLSNPPSAGPIVVHCSAGAG 1110
Cdd:cd18533    76 ELVSEEenDDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKreLNDSASLDPPIIVHCSAGVG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1111 RTGCYIVIDIMLDMAER--------EGVVD-IYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd18533   155 RTGTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 931-1158 5.41e-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: 5.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1010
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIP------GNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1011 VEVGRVKCYKYWPDDTE--VYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI 1087
Cdd:cd14617    75 VEKGRVKCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1088 RRVK--LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14617   155 RTVRdyINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 923-1163 6.48e-71

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: 238.63  E-value: 6.48e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  923 KKDQNRAKNRYGNIIAYDHSRVILQPVEDD-PSSDYINANYIDIWLYRDGyQRPSHYIATQGPVHETVYDFWRMIWQEQS 1001
Cdd:cd14606    14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQLLGPD-ENAKTYIASQGCLEATVNDFWQMAWQENS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1002 ACIVMVTNLVEVGRVKCYKYWPD--DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNE-IREVKQFHFTGWPDHGVPY 1078
Cdd:cd14606    93 RVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDHGVPS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1079 HATGLLSFIRRV--KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQ 1153
Cdd:cd14606   173 EPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252

                         250
                  ....*....|
gi 634743231 1154 YIFIHDAILE 1163
Cdd:cd14606   253 YKFIYVAIAQ 262
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 927-1162 2.19e-70

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: 236.32  E-value: 2.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIP------GYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEVGRVKCYKYWP--DDTEVYGDFKVTCVEMEPLAEYVVRTFtleRRGY-NEIREVKQFHFTGWPDHGVPY--HAT 1081
Cdd:cd14614    86 LTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREF---RVSYaDEVQDVMHFNYTAWPDHGVPTanAAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1082 GLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:cd14614   163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 634743231 1162 L 1162
Cdd:cd14614   243 Q 243
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 957-1164 8.07e-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: 8.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE----VYGDF 1032
Cdd:cd14538     1 YINASHIRIPVGGDTY----HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1033 KVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRT 1112
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 634743231 1113 GCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1164
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 931-1162 1.50e-69

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: 233.30  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1010
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIP------GYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1011 VEVGRVKCYKYWPDDTE--VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIR 1088
Cdd:cd14618    75 MENGRVLCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1089 RVK--LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1162
Cdd:cd14618   155 LVRehVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 957-1158 4.15e-69

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: 230.87  E-value: 4.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFK 1033
Cdd:cd14557     1 YINASYID------GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAEYVVRTFTL--ERRGYNEiREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGR 1111
Cdd:cd14557    75 VKINEEKICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 634743231 1112 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14557   154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 956-1164 1.34e-67

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: 226.83  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDIWLyrdgyqrPSH-----YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DTEV 1028
Cdd:cd14541     1 DYINANYVNMEI-------PGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1029 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 1108
Cdd:cd14541    74 FGNLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1109 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1164
Cdd:cd14541   154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1252-1453 2.18e-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: 2.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLS--QGCPQYWPEEGM--LRYGPIQVECMSC 1327
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKgrEKCERYWPEEGGkpLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1328 SMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECEegeGRTIIHCLNGGGRSG 1407
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES--REVTHLHYTGWPDHG-VPSSPEDLLALVRRVRKEARKPN---GPIVVHCSAGVGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1408 MFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd00047   155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 927-1163 1.64e-64

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: 221.14  E-value: 1.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEVGRVKCYKYWPDDTEV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLS 1085
Cdd:cd14628   126 LTKLREMGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1086 FIRRVKLSNPP--SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14628   206 FIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 927-1163 3.02e-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: 220.37  E-value: 3.02e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEVGRVKCYKYWPDDTEV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLS 1085
Cdd:cd14627   127 LTKLREMGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1086 FIRRVKLSNPP--SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14627   207 FIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 931-1158 2.68e-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: 215.16  E-value: 2.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  931 NRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNL 1010
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYIS------GYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1011 VEVGRVKCYKYWPDDTE---VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIreVKQFHFTGWPDHGVPYHATGLLSFI 1087
Cdd:cd14616    75 FEKGRIRCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1088 RRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14616   153 KLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 904-1163 6.53e-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: 216.46  E-value: 6.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  904 FKEEYESF--FEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIdiwlyRDGYQRPSHYIAT 981
Cdd:cd14610    19 LEKEWEALcaYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI-----MDHDPRNPAYIAT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  982 QGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAE-YVVRTFTLERRGYNE 1059
Cdd:cd14610    94 QGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1060 IREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVK 1138
Cdd:cd14610   174 TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLE 253

                         250       260
                  ....*....|....*....|....*
gi 634743231 1139 ALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14610   254 HLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 957-1161 1.08e-62

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: 212.51  E-value: 1.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV-YGDFKVT 1035
Cdd:cd14552     1 YINASFID------GYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA-GPIVVHCSAGAGRTGC 1114
Cdd:cd14552    75 LKDQTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 634743231 1115 YIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 930-1161 1.27e-62

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: 214.34  E-value: 1.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVIL-QPVEDDPSSDYINANYIDiwlyrdGY-QRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV 1007
Cdd:cd14613    28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIR------GYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1008 TNLVEVGRvKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSFI 1087
Cdd:cd14613   102 TNIEEMNE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 634743231 1088 RRV---KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:cd14613   179 QEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 926-1162 2.37e-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: 2.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  926 QNRAKNRYGNIIAYDHSRVILqpvedDPSSDYINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIV 1005
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFIKMPVGDEEFV----YIACQGPLPTTVADFWQMVWEQKSTVIA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1006 MVTNLVEVGRVKCYKYWPDD----TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHAT 1081
Cdd:cd14597    73 MMTQEVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1082 GLLSFIRRVKlsNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:cd14597   153 QLLTFISYMR--HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  .
gi 634743231 1162 L 1162
Cdd:cd14597   231 L 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 927-1163 4.21e-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: 214.20  E-value: 4.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  927 NRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFID------GYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEVGRVKCYKYWPDDTEV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLS 1085
Cdd:cd14629   127 LTKLREMGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1086 FIRRVKLSNPP--SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14629   207 FIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 920-1161 5.77e-62

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: 214.03  E-value: 5.77e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  920 DVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQE 999
Cdd:cd14604    50 ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIK------GVYGPKAYIATQGPLANTVIDFWRMIWEY 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1000 QSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGV 1076
Cdd:cd14604   124 NVAIIVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1077 PYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEE 1152
Cdd:cd14604   202 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKE 280


                  ....*....
gi 634743231 1153 QYIFIHDAI 1161
Cdd:cd14604   281 QYELVHRAI 289
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 929-1158 4.61e-61

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: 209.69  E-value: 4.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  929 AKNRYGNIIAYDHSRVILQ-PVEDDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVM 1006
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIR------GYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1007 VTNLVEvGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSF 1086
Cdd:cd14612    91 ITKLKE-KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1087 IRRVK--LSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14612   168 VAEVEesRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 932-1163 2.66e-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: 206.82  E-value: 2.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  932 RYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLV 1011
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFID------GYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1012 EVGRVKCYKYWPDDTEV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV 1090
Cdd:cd14623    75 ERGQEKCAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1091 KLSNPPSAG-PIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14623   155 QKQQQQSGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 910-1163 4.64e-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: 4.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  910 SFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETV 989
Cdd:cd14603    13 AFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIK------GVDGSRAYIATQGPLSHTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  990 YDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP--DDTEVYGDFKVTCV-EMEPLAEYVVRTFTLERRgyNEIREVKQF 1066
Cdd:cd14603    87 LDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1067 HFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVD---IYNCVKALRSR 1143
Cdd:cd14603   165 QYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQ 244

                         250       260
                  ....*....|....*....|
gi 634743231 1144 RINMVQTEEQYIFIHDAILE 1163
Cdd:cd14603   245 RPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 930-1158 2.77e-59

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: 203.61  E-value: 2.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVILQPVE-DDPSSDYINANYIDiwlyrdGYQ-RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV 1007
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIR------GYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1008 TNLVEVGRvKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGynEIREVKQFHFTGWPDHGVPYHATGLLSFI 1087
Cdd:cd14611    76 TKLKEKNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1088 RRVKLS--NPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14611   153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 957-1159 6.68e-59

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: 201.47  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTC 1036
Cdd:cd14558     1 YINASFID------GYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1037 VEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNP------PSAGPIVVHCSAGAG 1110
Cdd:cd14558    75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1111 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd14558   155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 930-1163 1.82e-58

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: 201.61  E-value: 1.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1009
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIK------GVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1010 LVEVGRVKCYKYWP---DDTEVYGDFKVTCVEMEPLAEYVVRTftLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF 1086
Cdd:cd14602    75 EFEMGKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILEL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1087 IRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAeREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1162
Cdd:cd14602   153 IWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  .
gi 634743231 1163 E 1163
Cdd:cd14602   232 E 232
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 32-192 2.28e-58

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: 198.34  E-value: 2.28e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231     32 SAGGCTFDDGPgACDYHQDLYDDFEWVHVSAQEP---HYLPPEMPQGSYMIVDSSDHDPGEKARLQLPTMKEN-DTHCID 107
Cdd:smart00137    2 SPGNCDFEEGS-TCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    108 FSYLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTfWPNEYQVIFEAEVSGGRSGYIAIDDIQV 187
Cdd:smart00137   81 FWYYMY---GSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 634743231    188 LSYPC 192
Cdd:smart00137  157 SNGPC 161
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 922-1162 2.38e-58

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: 202.77  E-value: 2.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  922 AKKDQNRAKNRYGNIIAYDHSRVILQpvEDDpssDYINANYIDIWLyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQS 1001
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVLQ--GNE---DYINASYVNMEI--PSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1002 ACIVMVTNLVEVGRVKCYKYWPDDTEV--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYH 1079
Cdd:cd14600   108 SLIVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1080 ATGLLSFIRRVKLSNPPSAgPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd14600   188 SSDFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                  ...
gi 634743231 1160 AIL 1162
Cdd:cd14600   267 AIL 269
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 906-1163 1.71e-57

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: 200.65  E-value: 1.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  906 EEYESF--FEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQpVEDDPS-SDYINANYIdiwlyRDGYQRPSHYIATQ 982
Cdd:cd14609    19 KEWQALcaYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLK-AESNPSrSDYINASPI-----IEHDPRMPAYIATQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  983 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKVTCVEMEPLAE-YVVRTFTLERRGYNEI 1060
Cdd:cd14609    93 GPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQET 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1061 REVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKA 1139
Cdd:cd14609   173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEH 252

                         250       260
                  ....*....|....*....|....
gi 634743231 1140 LRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14609   253 VRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 930-1156 7.35e-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: 196.84  E-value: 7.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVILQpvEDDPSSDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1009
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVK--LKQGDNDYINASLVEV----EEAKR--SYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1010 LVEVGRVKCYKYWPDDtEVYG------DFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGL 1083
Cdd:cd14545    73 LMEKGQIKCAQYWPQG-EGNAmifedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAF 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 634743231 1084 LSFIRRVKLSN--PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGV--VDIYNCVKALRSRRINMVQTEEQYIF 1156
Cdd:cd14545   152 LNFLQKVRESGslSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PHA02738 PHA02738
hypothetical protein; Provisional
 881-1161 4.30e-56

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 197.84  E-value: 4.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  881 HPAIRVADLLqhiNLMKTSDsygFKE----EYESFF-EGQSASWDVAKKdqNRAKNRYGNIIAYDHSRVILqPVEDDpSS 955
Cdd:PHA02738    6 FRELKYAEFL---ALMEKSD---CEEvitrEHQKVIsEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVIL-PAERN-RG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD---DTEVYGDF 1032
Cdd:PHA02738   76 DYINANYVD------GFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveqGSIRFGKF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1033 KVTCVEMEPLAEYVVRTFTLErRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK----------------LSNPP 1096
Cdd:PHA02738  150 KITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRqcqkelaqeslqighnRLQPP 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1097 sagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
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 ...
 957-1163 7.74e-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: 193.04  E-value: 7.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIdiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKVT 1035
Cdd:cd14546     1 YINASTI-----YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CV-EMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGC 1114
Cdd:cd14546    76 LVsEHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 634743231 1115 YIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14546   156 YILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 957-1158 9.27e-56

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: 192.64  E-value: 9.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP---DDTEVYGDFK 1033
Cdd:cd14542     1 YINANFIK------GVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPeegEEQLQFGPFK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAE-YVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRT 1112
Cdd:cd14542    75 ISLEKEKRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRT 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1113 GCYIVIDIMLDMAEREGVVD---IYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd14542   153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1218-1456 1.20e-54

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: 190.81  E-value: 1.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1218 ACLPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML 1296
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1297 ---NEVDLSQgCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWAShREVPGSKRS 1373
Cdd:cd14554    81 tklREMGREK-CHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1374 FLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14554   157 FIDFIGQVHKTKEQFGQ-EGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                  ...
gi 634743231 1454 VAL 1456
Cdd:cd14554   236 AAL 238
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 956-1161 4.53e-54

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: 187.91  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV-YGDFKV 1034
Cdd:cd14622     1 DYINASFID------GYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAG-PIVVHCSAGAGRTG 1113
Cdd:cd14622    75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1114 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 957-1163 7.79e-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: 187.66  E-value: 7.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDIWLyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-----DTEVYGD 1031
Cdd:cd14540     1 YINASHITATV--GGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggehDALTFGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1032 FKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF------IRR-----VKLSNPPSagP 1100
Cdd:cd14540    77 YKVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRhtnqdVAGHNRNP--P 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1101 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14540   155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 921-1172 1.24e-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: 189.47  E-value: 1.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  921 VAKKDQNRAKNRYGNIIAYDHSRVILQpVEDDpssDYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDFWRMIWQEQ 1000
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLH-QEDN---DYINASLIKM----EEAQR--SYILTQGPLPNTCGHFWEMVWEQK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1001 SACIVMVTNLVEVGRVKCYKYWPDDTE---VYGD--FKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHG 1075
Cdd:cd14608    89 SRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1076 VPYHATGLLSFIRRVKLSNP--PSAGPIVVHCSAGAGRTGCYIVID---IMLDMAEREGVVDIYNCVKALRSRRINMVQT 1150
Cdd:cd14608   169 VPESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQT 248

                         250       260
                  ....*....|....*....|....
gi 634743231 1151 EEQYIFIHDAILEAC--LCGETAI 1172
Cdd:cd14608   249 ADQLRFSYLAVIEGAkfIMGDSSV 272
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 913-1161 8.68e-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: 186.33  E-value: 8.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  913 EGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDpssdYINANYIDIwlyrDGYQRpsHYIATQGPVHETVYDF 992
Cdd:cd14607    10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVI----EEAQR--SYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  993 WRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAE-----YVVRTFTLERRGYNEIREVKQFH 1067
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKETGFSVKLLSEdvksyYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1068 FTGWPDHGVPYHATGLLSFIRRVKLSNP--PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREG--VVDIYNCVKALRSR 1143
Cdd:cd14607   160 YTTWPDFGVPESPASFLNFLFKVRESGSlsPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKY 239

                         250
                  ....*....|....*...
gi 634743231 1144 RINMVQTEEQYIFIHDAI 1161
Cdd:cd14607   240 RMGLIQTPDQLRFSYMAV 257
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 956-1163 9.71e-53

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: 184.38  E-value: 9.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  956 DYINANYIDIWLYRDGYQRpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD--DTEVYGDFK 1033
Cdd:cd14601     1 DYINANYINMEIPSSSIIN--RYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG 1113
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 634743231 1114 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 957-1164 3.18e-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: 182.64  E-value: 3.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD---DTEVYGDFK 1033
Cdd:cd14596     1 YINASYITMPVGEEEL----FYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPMELENYQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNppSAGPIVVHCSAGAGRTG 1113
Cdd:cd14596    77 LRLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1114 CYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 1164
Cdd:cd14596   155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1252-1453 4.48e-52

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: 181.82  E-value: 4.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNevDLSQG----CPQYWPEEGMlRYGPIQVECMSC 1327
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLT--ELKEGdqeqCAQYWGDEKK-TYGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1328 SMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEGEGRT---IIHCLNGGG 1404
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKGE-ELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1405 RSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14558   155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1252-1454 4.88e-52

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 181.70  E-value: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLSQG-CPQYWPEEGMLRYGPIQVEcMSCSM 1329
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIkERSQNkCAQYWPEDGSVSSGDITVE-LKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 DCDVINriFRICNLTRPQEGYL-MVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEEceEGEGRTIIHCLNGGGRSGM 1408
Cdd:cd14552    80 DYEDYT--LRDFLVTKGKGGSTrTVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1409 FCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDV 1454
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 36-192 1.08e-51

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: 179.10  E-value: 1.08e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    36 CTFDDGPgACDYHQDLYDDFEWVHVSAQEPHYLPPE-----MPQGSYMIVDSSDHDPGEKARLQLPTMKENDT-HCIDFS 109
Cdd:pfam00629    1 CDFEDGN-LCGWTQDSSDDFDWERVSGPSVKTGPSSdhtqgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   110 YLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFwPNEYQVIFEAEVSGGRSGYIAIDDIQVLS 189
Cdd:pfam00629   80 YHMS---GSGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ...
gi 634743231   190 YPC 192
Cdd:pfam00629  156 GPC 158
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 36-192 2.86e-51

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: 177.96  E-value: 2.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   36 CTFDDGpgACDYHQDLYDDFEWVHVSAQEPHYLPP-----EMPQGSYMIVDSSDHDPGEKARLQLPTMKEN-DTHCIDFS 109
Cdd:cd06263     1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  110 YLLYsqkGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWpNEYQVIFEAEVSGGRSGYIAIDDIQVLS 189
Cdd:cd06263    79 YHMY---GSGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 634743231  190 YPC 192
Cdd:cd06263   155 GPC 157
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1251-1458 6.90e-49

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 172.88  E-value: 6.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1251 NYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--SQGCPQYWPEEGMLRYGPIQVECMSCS 1328
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEreQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1329 MdCDVINriFRICNLTRPQEGYL-MVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEEceEGEGRTIIHCLNGGGRSG 1407
Cdd:cd14622    81 L-LETIS--IRDFLVTYNQEKQTrLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1408 MFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEY 1458
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1170-1461 1.79e-48

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 174.92  E-value: 1.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1170 TAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSvtPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDG-E 1248
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLAS--SKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1249 SSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--SQGCPQYWPEEGMLRYGPIQVECMS 1326
Cdd:cd14628    79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmgREKCHQYWPAERSARYQYFVVDPMA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1327 csmDCDVINRIFRICNLTRPQEGY-LMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECEEgEGRTIIHCLNGGGR 1405
Cdd:cd14628   159 ---EYNMPQYILREFKVTDARDGQsRTVRQFQFTDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPISVHCSAGVGR 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1406 SGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLES 1461
Cdd:cd14628   234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 904-1163 1.79e-48

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 175.58  E-value: 1.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  904 FKEEYESFFEGQSA-SWDVAKKDQNRAKNRYGNIIAYDHSRVILqPVEDDpSSDYINANYIDiwlyrdGYQRPSHYIATQ 982
Cdd:PHA02742   28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVIL-KIEDG-GDDFINASYVD------GHNAKGRFICTQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  983 GPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW---PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNE 1059
Cdd:PHA02742  100 APLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1060 IREVKQFHFTGWPDHGVPYHATGLLSFIRRV-----------KLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE 1128
Cdd:PHA02742  180 SLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNER 259

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 634743231 1129 GVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:PHA02742  260 AIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1218-1461 2.76e-47

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 171.45  E-value: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1218 ACLPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML 1296
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1297 NEVDL--SQGCPQYWPEEGMLRYGPIQVECMScsmDCDVINRIFRICNLTRPQEGY-LMVQQFQYLGWaSHREVPGSKRS 1373
Cdd:cd14627   128 TKLREmgREKCHQYWPAERSARYQYFVVDPMA---EYNMPQYILREFKVTDARDGQsRTVRQFQFTDW-PEQGVPKSGEG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1374 FLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14627   204 FIDFIGQVHKTKEQFGQ-DGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQ 282


                  ....*...
gi 634743231 1454 VALEYLES 1461
Cdd:cd14627   283 AALEYLGS 290
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 926-1163 4.37e-47

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: 170.95  E-value: 4.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  926 QNRAKNRYGNIIAYDHSRVILQPVEDDPSSdYINANYIDIWLYRDGYqrpsHYIATQGPVHETVYDFWRMIWQEQSACIV 1005
Cdd:cd14599    37 ENAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEW----HYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1006 MVTNLVEVGRVKCYKYWPD-----DTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHA 1080
Cdd:cd14599   112 MVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1081 TGLLSF------IRR--------VKLSNPpsagPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRIN 1146
Cdd:cd14599   192 QGFLSYleeiqsVRRhtnsmldsTKNCNP----PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMF 267

                         250
                  ....*....|....*..
gi 634743231 1147 MVQTEEQYIFIHDAILE 1163
Cdd:cd14599   268 MIQTIAQYKFVYQVLIQ 284
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1218-1461 6.83e-47

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: 170.29  E-value: 6.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1218 ACLPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML 1296
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1297 NEVDL--SQGCPQYWPEEGMLRYGPIQVECMScsmDCDVINRIFRICNLTRPQEGY-LMVQQFQYLGWaSHREVPGSKRS 1373
Cdd:cd14629   128 TKLREmgREKCHQYWPAERSARYQYFVVDPMA---EYNMPQYILREFKVTDARDGQsRTIRQFQFTDW-PEQGVPKTGEG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1374 FLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14629   204 FIDFIGQVHKTKEQFGQ-DGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYR 282


                  ....*...
gi 634743231 1454 VALEYLES 1461
Cdd:cd14629   283 AALEYLGS 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 906-1158 1.12e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 167.49  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  906 EEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQpVEDDPSSDYINANYIDiwlyrdGYQRPSHYIATQGPV 985
Cdd:PHA02747   30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILD-SGGGSTSDYIHANWID------GFEDDKKFIATQGPF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  986 HETVYDFWRMIWQEQSACIVMVTNLVEV-GRVKCYKYW---PDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIR 1061
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1062 EVKQFHFTGWPDHGVPYHATGLLSFIRRV--------KLSNPPSA--GPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1131
Cdd:PHA02747  183 KISHFQCSEWFEDETPSDHPDFIKFIKIIdinrkksgKLFNPKDAllCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI 262

                         250       260
                  ....*....|....*....|....*..
gi 634743231 1132 DIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:PHA02747  263 CLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 957-1159 1.34e-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: 163.35  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVKCYKYWPDDTE-VYGDFKVT 1035
Cdd:cd14556     1 YINAALLD------SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTLER--RGYNEIREVKQFHFTGWPDHG-VPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSAGAGR 1111
Cdd:cd14556    74 FVSTTIDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1112 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd14556   154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1248-1457 2.36e-45

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 163.68  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1248 ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDL--SQGCPQYWPEEGMLRYGPIQVEcM 1325
Cdd:cd14623    22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGDITIE-L 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1326 SCSMDCDVIN-RIFRICNlTRPQEGYlMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEEceEGEGRTIIHCLNGGG 1404
Cdd:cd14623   101 KKEEECESYTvRDLLVTN-TRENKSR-QIRQFHFHGWP-EVGIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1405 RSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14623   176 RTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 957-1158 8.20e-44

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: 158.40  E-value: 8.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE-VGRVKCYKYWPD---DTEVYGDF 1032
Cdd:cd17658     1 YINASLVE----TPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAeenESREFGRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1033 KVTCVEMEplaeyvVRTFTLERRG----YNEIRE----VKQFHFTGWPDHGVPYHATGLLSFIRRVKLSnPPSAGPIVVH 1104
Cdd:cd17658    77 SVTNKKLK------HSQHSITLRVlevqYIESEEpplsVLHIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1105 CSAGAGRTGCYIVID-----IML-DMAeregVVDIYNCVKALRSRRINMVQTEEQYIFIH 1158
Cdd:cd17658   150 CSAGIGRTGAYCTIHntirrILEgDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
930-1157 4.42e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 4.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  930 KNRYGNIIAYDHSRVilqpVEDDPssdYINANYIDIwlyRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTN 1009
Cdd:COG5599    45 LNRFRDIQPYKETAL----RANLG---YLNANYIQV---IGNHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1010 LVEVG--RVKCYKYWPDDTEvYGDFKV--TCVEMEPLAEYV-VRTFTLERRGYN-EIREVKQFHFTGWPDHGVPyHATGL 1083
Cdd:COG5599   111 DDEISkpKVKMPVYFRQDGE-YGKYEVssELTESIQLRDGIeARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAI-SAEAL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1084 LSFIRRV----KLSNPPSaGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDIYNCVKALR-SRRINMVQTEEQYIF 1156
Cdd:COG5599   189 KNLADLIdkkeKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDV 267


                  .
gi 634743231 1157 I 1157
Cdd:COG5599   268 L 268
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1228-1450 1.54e-42

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: 155.20  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1228 RFMDMLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG-- 1304
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQC-MEKGrv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 -CPQYWPE-EGMLRYGPIQVECMSCSMDCDVINRIFRICNltrpQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLilqVE 1382
Cdd:cd14548    80 kCDHYWPFdQDPVYYGDITVTMLSESVLPDWTIREFKLER----GDEVRSVRQFHFTAWPDH-GVPEAPDSLLRF---VR 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1383 KWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14548   152 LVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 957-1159 1.96e-42

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: 154.46  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---TEVYGDFK 1033
Cdd:cd14539     1 YINASLIE-----DLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1034 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---LSNPPSAGPIVVHCSAGAG 1110
Cdd:cd14539    76 VSLQSVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshyLQQRSLQTPIVVHCSSGVG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 634743231 1111 RTGCY-IVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHD 1159
Cdd:cd14539   156 RTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 957-1163 1.10e-41

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: 152.82  E-value: 1.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDIWLYRDGYQrpshYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-----DDTEVYGD 1031
Cdd:cd14598     1 YINASHIKVTVGGKEWD----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1032 FKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--------LSNPPSAG-PIV 1102
Cdd:cd14598    77 FKITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnsTIDPKSPNpPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1103 VHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1214-1452 1.57e-41

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: 154.06  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1214 DCSIAclPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTS 1292
Cdd:cd14543    22 LCSLA--PANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1293 IVMLNEVDlSQG---CPQYWPEEG--MLRYGPIQVECMSCSMDCDVINRIFRICNL----TRPqegylmVQQFQYLGWAS 1363
Cdd:cd14543   100 IVMTTRVV-ERGrvkCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTetdeSRQ------VTHFQFTSWPD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1364 HrEVPGSKRSFLKLILQVEKWQEECEEGEGRT----------IIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKT 1433
Cdd:cd14543   173 F-GVPSSAAALLDFLGEVRQQQALAVKAMGDRwkghppgppiVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRR 251

                         250
                  ....*....|....*....
gi 634743231 1434 LRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14543   252 MRTQRAFSIQTPDQYYFCY 270
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1062-1163 4.46e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 146.73  E-value: 4.46e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1062 EVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1138
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 634743231   1139 ALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1062-1163 4.46e-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: 4.46e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1062 EVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSA--GPIVVHCSAGAGRTGCYIVIDIMLDMAERE-GVVDIYNCVK 1138
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 634743231   1139 ALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1223-1457 1.02e-40

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: 150.62  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN--EV 1299
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTklEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1300 DLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNL--TRPQEgylmVQQFQYLGWASHrEVPGSKRSFLKL 1377
Cdd:cd14553    83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKRE----VRQFQFTAWPDH-GVPEHPTPFLAF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1378 ILQVekwQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14553   158 LRRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 924-1161 2.91e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 152.11  E-value: 2.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  924 KDQNRAKNRYGNIIAYDHSRVILQPVE-------------------DDPSSDYINANYIDiwlyrdGYQRPSHYIATQGP 984
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkievtsEDNAENYIHANFVD------GFKEANKFICAQGP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  985 VHETVYDFWRMIWQEQSACIVMVTNlVEVGRVKCYKYW--PDDTEV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIR 1061
Cdd:PHA02746  122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1062 EVKQFHFTGWPDHGVPYHATGLLSFIRRVKL----------SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVV 1131
Cdd:PHA02746  201 EIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV 280

                         250       260       270
                  ....*....|....*....|....*....|
gi 634743231 1132 DIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:PHA02746  281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1188-1450 1.28e-38

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: 146.35  E-value: 1.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1188 DSQTNSSHLKDEFQTLNSvtprLQAED--CSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGES-SNYINAA-LMDSYRQ 1263
Cdd:cd14610    11 DHLKNKNRLEKEWEALCA----YQAEPnaTNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1264 PAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLSQgCPQYWPEEGMLRYGPIQVECMSCSMDC-DVINRIFR 1339
Cdd:cd14610    87 NPAYIATQGPLPATVADFWQMVWESGCVVIVMLTplaENGVKQ-CYHYWPDEGSNLYHIYEVNLVSEHIWCeDFLVRSFY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1340 ICNLTRPQEgyLMVQQFQYLGWASHReVPGSKRSFLKLILQVEKwqeeCEEGEG-RTIIHCLNGGGRSGMFCAIGIVV-E 1417
Cdd:cd14610   166 LKNLQTNET--RTVTQFHFLSWNDQG-VPASTRSLLDFRRKVNK----CYRGRScPIIVHCSDGAGRSGTYILIDMVLnK 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 634743231 1418 MVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14610   239 MAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1252-1457 3.92e-37

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


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 139.28  E-value: 3.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPEEGMLrYGPIQVECMSCSM 1329
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRvKCSRYWPDDTEV-YGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 DCDVINRIFricnlTRPQEGY---LMVQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECEEGEGRTIIHCLNGGGRS 1406
Cdd:cd14555    80 LAEYVVRTF-----ALERRGYheiREVRQFHFTGWPDH-GVPYHATGLLGFIRRV---KASNPPSAGPIVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1407 GMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14555   151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1252-1452 3.56e-36

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: 136.30  E-value: 3.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEG-MLRYGPIQV-----ECM 1325
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEkPLECETFKVtlsgeDHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1326 SCSMDCDVINRIFRICNltrPQEGY-LMVQQFQYLGWAshrEVPGSKRSFLKLILQVekwQEECEEGEGRTIIHCLNGGG 1404
Cdd:cd14550    81 CLSNEIRLIVRDFILES---TQDDYvLEVRQFQCPSWP---NPCSPIHTVFELINTV---QEWAQQRDGPIVVHDRYGGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1405 RSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14550   152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1223-1457 5.13e-36

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


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 137.08  E-value: 5.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVD 1300
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1301 LSQ-GCPQYWPEEGMLrYGPIQVECMSCSMDCDVINRIFricnlTRPQEGY---LMVQQFQYLGWASHrEVPGSKRSFLK 1376
Cdd:cd14630    83 VGRvKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTF-----TVQKKGYheiREIRQFHFTSWPDH-GVPCYATGLLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1377 LILQVeKWQEECEEGEgrTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd14630   156 FVRQV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232


                  .
gi 634743231 1457 E 1457
Cdd:cd14630   233 E 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1199-1452 7.76e-36

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: 137.65  E-value: 7.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1199 EFQTLNSVTPRLQAED---CSIACLPRNHDKNRFMDMLPPDR---CLPFLItiDGESSNYINAALMDSYRQPAAFIVTQY 1272
Cdd:cd14603     3 EFSEIRACSAAFKADYvcsTVAGGRKENVKKNRYKDILPYDQtrvILSLLQ--EEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1273 PLPNTVKDFWRLVYDYGCTSIVM-LNEVDLS-QGCPQYWP-EEGMLRYGPIQVECMSCS-MDCDVINRIFRI--CNLTRp 1346
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMaCREIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKVtfQKESR- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1347 qegylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeeceeGEGRT--IIHCLNGGGRSGMFCAIGIVVEMVKRQNV 1424
Cdd:cd14603   160 -----SVSHFQYMAWPDH-GIPDSPDCMLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRI 228

                         250       260       270
                  ....*....|....*....|....*....|.
gi 634743231 1425 VD---VFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14603   229 PPdfsIFDVVLEMRKQRPAAVQTEEQYEFLY 259
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1223-1457 9.86e-36

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 137.47  E-value: 9.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDL 1301
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1302 SQ--GCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASH--REVPGSKRSFLKL 1377
Cdd:cd14626   121 KSrvKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDHgvPEYPTPILAFLRR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1378 IlqvekwqEECEEGE-GRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd14626   199 V-------KACNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271


                  .
gi 634743231 1457 E 1457
Cdd:cd14626   272 E 272
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1252-1453 1.05e-35

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 135.17  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDlsQG---CPQYWPEEGMLRYGPIQVECMSC 1327
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMItNLVE--RGrrkCDQYWPKEGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1328 -SMDCDVInRIFRICNL----TRPQEGYLMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNG 1402
Cdd:cd14549    79 eVLATYTV-RTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH----GVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1403 GGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14549   154 VGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1227-1456 1.15e-35

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: 135.84  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNeVDLSQG- 1304
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLT-VGMENGr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 --CPQYWPEEGM-LRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYlmVQQFQYLGWASHrEVPGSKRSFLKLilqV 1381
Cdd:cd14618    80 vlCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERR--VKHLHYTAWPDH-GIPESTSSLMAF---R 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 634743231 1382 EKWQEECE--EGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd14618   154 ELVREHVQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1227-1457 2.79e-35

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: 134.56  E-value: 2.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG-- 1304
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC-VEQGrt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 -CPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEK 1383
Cdd:cd14615    80 kCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESR--TVRHFHFTSWPDH-GVPETTDLLINFRHLVRE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1384 WQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14615   157 YMKQNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1231-1457 3.01e-35

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: 134.68  E-value: 3.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1231 DMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVD--LSQGCPQ 1307
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1308 YWPEEGMLRYGPIQVECMSCSMDCDVINRIFRI----CNLTRPQEgylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEK 1383
Cdd:cd14620    83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIqpqlPDGCKAPR---LVTQLHFTSWPDF-GVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1384 WQeecEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14620   159 VN---PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1188-1450 3.12e-35

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: 136.32  E-value: 3.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1188 DSQTNSSHLKDEFQTLNSvtprLQAE--DCSIACLPRNHDKNRFMDMLPPDRC-LPFLITIDGESSNYINAALMDSY--R 1262
Cdd:cd14609     9 DHLRNRDRLAKEWQALCA----YQAEpnTCSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASPIIEHdpR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1263 QPAaFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLSQGCPQYWPEEGMLRYGPIQVECMSCSMDC-DVINRIFR 1339
Cdd:cd14609    85 MPA-YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCeDFLVRSFY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1340 ICNLtRPQEGYLMVqQFQYLGWASHrEVPGSKRSFLKLILQVEKwqeeCEEGEGRTII-HCLNGGGRSGMFCAIGIVV-E 1417
Cdd:cd14609   164 LKNV-QTQETRTLT-QFHFLSWPAE-GIPSSTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGRTGTYILIDMVLnR 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 634743231 1418 MVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14609   237 MAKGVKEIDIAATLEHVRDQRPGMVRTKDQFEF 269
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1246-1457 3.66e-35

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 133.99  E-value: 3.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1246 DGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPEEGMLrYGPIQVE 1323
Cdd:cd14631     9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRvKCYKYWPDDTEV-YGDFKVT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1324 CMSCSMDCDVINRIFRICNltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEceeGEGRTIIHCLNGG 1403
Cdd:cd14631    88 CVEMEPLAEYVVRTFTLER--RGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRVKLSNPP---SAGPIVVHCSAGA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1404 GRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14631   162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1227-1450 1.31e-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: 132.52  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDR---CLPflITIDGESSNYINAALMDSYR-QPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDL 1301
Cdd:cd14547     1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMItNLTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1302 SQGCPQYWPEEGMLRYGPIQVecmscsmdcdVINRI-----FRICNLT-RPQEGYLMVQQFQYLGWASHrEVPGSKRSFL 1375
Cdd:cd14547    79 KEKCAQYWPEEENETYGDFEV----------TVQSVketdgYTVRKLTlKYGGEKRYLKHYWYTSWPDH-KTPEAAQPLL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1376 KLILQVEKWQEEcEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14547   148 SLVQEVEEARQT-EPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1223-1457 5.01e-34

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 132.47  E-value: 5.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVD 1300
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1301 LSQ-GCPQYWPEEGMLrYGPIQVECMSCSMDCDVINRIFRIcnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLIL 1379
Cdd:cd14633   120 VGRvKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1380 QVekwQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14633   196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1252-1452 7.95e-34

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: 129.47  E-value: 7.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPEEG--MLRYGPIQVECMSC 1327
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKkKCERYWPEEGeeQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1328 SMDCDVInrIFRICNLTRPQEGYlMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecEEGEGRTIIHCLNGGGRSG 1407
Cdd:cd14542    81 KRVGPDF--LIRTLKVTFQKESR-TVYQFHYTAWPDH-GVPSSVDPILDLVRLVRDYQ---GSEDVPICVHCSAGCGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1408 MFCAIGIVVEMVKRQNVVD---VFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14542   154 TICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1252-1457 8.09e-34

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: 129.79  E-value: 8.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLSQ-GCPQYWPEEGMLrYGPIQVECMSCSM 1329
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlVEVGRvKCSKYWPDDSDT-YGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 DCDVINRIFricnlTRPQEGYLM---VQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECEEGEGRTIIHCLNGGGRS 1406
Cdd:cd14632    80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVVHCSAGAGRT 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1407 GMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1220-1457 1.27e-33

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: 131.75  E-value: 1.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1220 LPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNE 1298
Cdd:cd14625    44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1299 VDLSQ--GCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLK 1376
Cdd:cd14625   124 LEEKSriKCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1377 LILQVEKwqeeCEEGE-GRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVA 1455
Cdd:cd14625   201 FLRRVKT----CNPPDaGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276


                  ..
gi 634743231 1456 LE 1457
Cdd:cd14625   277 LE 278
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1226-1457 2.21e-33

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: 129.57  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1226 KNRFMDMLPPDRCLP--FLITIDgESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVM-LNEVDLS 1302
Cdd:cd14602     1 KNRYKDILPYDHSRVelSLITSD-EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMaCMEFEMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1303 -QGCPQYWPEEG--MLRYGPIQVECMSCSMDCDVINRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLIL 1379
Cdd:cd14602    80 kKKCERYWAEPGemQLEFGPFSVTCEAEKRKSDYIIRTLKV----KFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1380 QVEKWQeecEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNV---VDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd14602   155 DVRCYQ---EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIpenFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  .
gi 634743231 1457 E 1457
Cdd:cd14602   232 E 232
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1218-1450 3.94e-33

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: 129.24  E-value: 3.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1218 ACLPRNHDKNRFMDMLPPDRCLPFLITI-DGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML 1296
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1297 NEVDLSQ--GCPQYWP-EEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgylmVQQFQYLGWASHrEVPGSKRS 1373
Cdd:cd14614    87 TQCNEKRrvKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDH-GVPTANAA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1374 flKLILQ-VEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14614   162 --ESILQfVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1225-1452 5.48e-33

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: 128.28  E-value: 5.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1225 DKNRFMDMLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLS 1302
Cdd:cd14545     2 NRYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmeKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1303 QGCPQYWP----EEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLI 1378
Cdd:cd14545    79 IKCAQYWPqgegNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1379 LQVEKwQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNV--VDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14545   156 QKVRE-SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1252-1452 1.51e-32

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: 126.02  E-value: 1.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALM--DSYRQPAaFIVTQYPLPNTVKDFWRLVYDYGCTSIVML---NEVDLSQgCPQYWPEEGMLRYGPIQVECMS 1326
Cdd:cd14546     1 YINASTIydHDPRNPA-YIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlQENGVKQ-CARYWPEEGSEVYHIYEVHLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1327 CSMDC-DVINRIFRICNL----TRpqegylMVQQFQYLGWaSHREVPGSKRSFLKLILQVEKwqeeCEEGEGRTII-HCL 1400
Cdd:cd14546    79 EHIWCdDYLVRSFYLKNLqtseTR------TVTQFHFLSW-PDEGIPASAKPLLEFRRKVNK----SYRGRSCPIVvHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1401 NGGGRSGMFCAIGIVVE-MVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14546   148 DGAGRTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVL 200
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1227-1459 1.86e-32

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: 126.93  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDRCLPFLITIDGE-SSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG- 1304
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNC-MEAGr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 --CPQYWPEEGM-LRYGPIQVECMSCSMDCDVINRIFRICNltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQV 1381
Cdd:cd14619    80 vkCEHYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLLKQ--VEEQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1382 EKWQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYL 1459
Cdd:cd14619   157 RQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1196-1458 4.35e-32

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: 127.83  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1196 LKDEFQTLnSVTPrLQAEdCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPL 1274
Cdd:cd14621    28 FREEFNAL-PACP-IQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1275 PNTVKDFWRLVYDYGCTSIVMLNEVDLSQ--GCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNL-----TRPQ 1347
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtnKKPQ 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1348 EgylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEegeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDV 1427
Cdd:cd14621   185 R---LITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYA---GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDV 257

                         250       260       270
                  ....*....|....*....|....*....|.
gi 634743231 1428 FHAVKTLRNSKPNMVEAPEQYRFCYDVALEY 1458
Cdd:cd14621   258 YGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 957-1163 5.56e-32

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: 124.37  E-value: 5.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMvtnLVEVGRVK-CYKYWPDDTEV-YGDFKV 1034
Cdd:cd14636     1 YINAALMD------SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQgCPQYWPEEGMLrYGPIQV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLAEYVVRTF-----TLERRGYneiREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHC 1105
Cdd:cd14636    72 ECMSCSMDCDVISRIFricnlTRPQEGY---LMVQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHC 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 634743231 1106 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14636   149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1252-1453 6.62e-32

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 124.28  E-value: 6.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAalmdSYRQPAA-----FIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN-EVDLSQG-CPQYWPEEGM-LRYGPIQVE 1323
Cdd:cd18533     1 YINA----SYITLPGtsskrYIATQGPLPATIGDFWKMIWQNNVGVIVMLTpLVENGREkCDQYWPSGEYeGEYGDLTVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1324 CMSCSM--DCDVINRIFRicnLTRPQEGYLMVQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECEEgEGRTIIHCLN 1401
Cdd:cd18533    77 LVSEEEndDGGFIVREFE---LSKEDGKVKKVYHIQYKSWPDFG-VPDSPEDLLTLIKLKRELNDSASL-DPPIIVHCSA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1402 GGGRSGMFCAIGIVVEMVKRQNVVD---------VFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd18533   152 GVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1223-1448 7.21e-32

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 126.97  E-value: 7.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRC-LPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVM-LNEVD 1300
Cdd:cd14604    57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMaCREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1301 LS-QGCPQYWPE--EGMLRYGPIQVECMSCSMDCDVINRIFricnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKL 1377
Cdd:cd14604   137 MGrKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRTL----LLEFQNETRRLYQFHYVNWPDH-DVPSSFDSILDM 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1378 ILQVEKWQEEceegEGRTI-IHCLNGGGRSGMFCAIGIVVEMVKRQNV---VDVFHAVKTLRNSKPNMVEAPEQY 1448
Cdd:cd14604   212 ISLMRKYQEH----EDVPIcIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQY 282
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 957-1163 1.64e-31

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 123.21  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDDTE-VYGDFKVT 1035
Cdd:cd14634     1 YINAALMD------SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRVKLSNPP---SAGPIVVHCSAGA 1109
Cdd:cd14634    73 FVSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1220-1457 2.38e-31

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: 125.23  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1220 LPRNHDKNRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNE 1298
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1299 VDLSQ--GCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLK 1376
Cdd:cd14624   124 LEERSrvKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1377 LILQVEKwqeeCEEGE-GRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVA 1455
Cdd:cd14624   201 FLRRVKT----CNPPDaGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                  ..
gi 634743231 1456 LE 1457
Cdd:cd14624   277 LE 278
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1252-1450 9.10e-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: 121.28  E-value: 9.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDsYRQPAAFIVTQY-----PLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG---CPQYWPEEG-MLRYGPIQV 1322
Cdd:cd14541     2 YINANYVN-MEIPGSGIVNRYiaaqgPLPNTCADFWQMVWEQKSTLIVMLTTL-VERGrvkCHQYWPDLGeTMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1323 ECMSCSMDCDVINRIFRICNLTRPQEGYlmVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEgegRTIIHCLNG 1402
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEERH--ITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRVGMVE---PTVVHCSAG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1403 GGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14541   154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1252-1452 9.58e-31

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 120.79  E-value: 9.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLSQGCPQYWPEEGMLRYGPIQVECMSCSM 1329
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTnlKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 DCDVINRIF------RICNLTRPQegylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecEEGEGRTIIHCLNGG 1403
Cdd:cd14551    81 LVDYTTRKFciqkvnRGIGEKRVR----LVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSAN---PPRAGPIVVHCSAGV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 634743231 1404 GRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14551   153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1223-1461 1.27e-30

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: 122.05  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLpfLITIDGE----SSNYINAALM--------DSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGC 1290
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDpnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1291 TSIVMLN-EVDLSQG-CPQYWPEEGMLR-YGPIQVECMSCSMDCDVINRIFRicnLTRPQEGYL--MVQQFQYLGWASHr 1365
Cdd:cd14605    80 RVIVMTTkEVERGKSkCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELK---LSKVGQGNTerTVWQYHFRTWPDH- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1366 EVPGSKRSFLKLILQVEKWQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNV---VDVFHAVKTLRNSKPNMV 1442
Cdd:cd14605   156 GVPSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMV 234

                         250
                  ....*....|....*....
gi 634743231 1443 EAPEQYRFCYDVALEYLES 1461
Cdd:cd14605   235 QTEAQYRFIYMAVQHYIET 253
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1226-1454 2.30e-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: 121.51  E-value: 2.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1226 KNRFMDMLPPDRCLPFLITIDGES--SNYINAALMDSY-RQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVD-L 1301
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEeM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1302 SQGCPQYWPEEGMLrYGPIQVECMSCSMDCDVINRIFRIcnltRPQEGYLMVQQFQYLGWASHReVPGSKRSFLKLILQV 1381
Cdd:cd14613   108 NEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-TPDNAPPLLQLVQEV 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1382 EKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDV 1454
Cdd:cd14613   182 EEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1226-1452 2.92e-30

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


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 120.02  E-value: 2.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1226 KNRFMDMLPPDRCLPFLIT--IDGESSNYINAALMDSYR-QPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEV-DL 1301
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1302 SQGCPQYWPEEGMLrYGPIQVeCMSCSMDCDVinriFRICNLTRPQEGYLM-VQQFQYLGWASHReVPGSKRSFLKLILQ 1380
Cdd:cd14611    82 NEKCVLYWPEKRGI-YGKVEV-LVNSVKECDN----YTIRNLTLKQGSQSRsVKHYWYTSWPDHK-TPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 634743231 1381 VEKWQEEcEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14611   155 VEEDRLA-SPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1220-1452 9.40e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 119.56  E-value: 9.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1220 LPRNHDKNRFMDMLP-PDR--CLPFLITIDgESSNYINAALMDSYR-QPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVM 1295
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1296 LNEV-DLSQGCPQYWPE-EGmlRYGP--IQVECMScsmDCDVinriFRICNLT-RPQEGYLMVQQFQYLGWASHrEVPGS 1370
Cdd:cd14612    91 ITKLkEKKEKCVHYWPEkEG--TYGRfeIRVQDMK---ECDG----YTIRDLTiQLEEESRSVKHYWFSSWPDH-QTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1371 KRSFLKLILQVEKwQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14612   161 AGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                  ..
gi 634743231 1451 CY 1452
Cdd:cd14612   240 LH 241
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1209-1457 1.16e-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: 120.13  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1209 RLQAED--CSIACLPRNHDKNRFMDMLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVY 1286
Cdd:cd14608     9 RHEASDfpCRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVW 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1287 DYGCTSIVMLNEVdLSQG---CPQYWPE----EGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMvqQFQYL 1359
Cdd:cd14608    86 EQKSRGVVMLNRV-MEKGslkCAQYWPQkeekEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL--HFHYT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1360 GWASHrEVPGSKRSFLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGI-VVEMVKRQN--VVDVFHAVKTLRN 1436
Cdd:cd14608   163 TWPDF-GVPESPASFLNFLFKVRESGSLSPE-HGPVVVHCSAGIGRSGTFCLADTcLLLMDKRKDpsSVDIKKVLLEMRK 240

                         250       260
                  ....*....|....*....|.
gi 634743231 1437 SKPNMVEAPEQYRFCYDVALE 1457
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVIE 261
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1227-1452 1.31e-29

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: 118.48  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDRCLPFLITIDGES-SNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG- 1304
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQC-VEKGr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 --CPQYWP-EEGMLRYGPIQVECMSCSMDCDVINRIFRICN---LTRPQegylMVQQFQYLGWASHrEVPGSKRSFLKLI 1378
Cdd:cd14617    80 vkCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSeeqLDAPR----LVRHFHYTVWPDH-GVPETTQSLIQFV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1379 LQVEKWQEEcEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd14617   155 RTVRDYINR-TPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1221-1457 3.44e-29

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: 118.60  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1221 PRNHDKNRFMDMLPPDRC---LPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN 1297
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1298 EVdLSQG---CPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICN--LTRPQEG-------YLMVQQFQYLGWASHr 1365
Cdd:cd17667   105 NL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKGnpkgrqnERTVIQYHYTQWPDM- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1366 evpGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAP 1445
Cdd:cd17667   183 ---GVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                         250
                  ....*....|..
gi 634743231 1446 EQYRFCYDVALE 1457
Cdd:cd17667   260 EQYIFIHDALLE 271
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1223-1461 6.27e-29

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: 117.18  E-value: 6.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLITIDGE--SSNYINA------ALMDSYRQPA-AFIVTQYPLPNTVKDFWRLVYDYGCTSI 1293
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirneNEGPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1294 VML-NEVDLSQG-CPQYWPEEGMLR-YGPIQVECMSCSMDCDVINRIFricNLTRPQEGYLM--VQQFQYLGWASHrEVP 1368
Cdd:cd14544    81 VMTtKEVERGKNkCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLREL---QVSKLDQGDPIreIWHYQYLSWPDH-GVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1369 GSKRSFLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNV---VDVFHAVKTLRNSKPNMVEAP 1445
Cdd:cd14544   157 SDPGGVLNFLEDVNQRQESLPH-AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTE 235

                         250
                  ....*....|....*.
gi 634743231 1446 EQYRFCYDVALEYLES 1461
Cdd:cd14544   236 AQYKFIYVAVAQYIET 251
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 957-1157 9.37e-29

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: 114.73  E-value: 9.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCykYWPDDTEV--YGDFKV 1034
Cdd:cd14550     1 YINASYLQ------GYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPleCETFKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 T-CVEMEPLAE----YVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGA 1109
Cdd:cd14550    73 TlSGEDHSCLSneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFI 1157
Cdd:cd14550   151 VQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1227-1450 4.20e-28

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 113.85  E-value: 4.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1227 NRFMDMLPPDRCLPFLITIDG-ESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG- 1304
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQC-FEKGr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1305 --CPQYWPEEG--MLRYGPIQVECMSCSMDCDVINRIFRIcnltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQ 1380
Cdd:cd14616    80 irCHQYWPEDNkpVTVFGDIVITKLMEDVQIDWTIRDLKI----ERHGDYMMVRQCNFTSWPEH-GVPESSAPLIHFVKL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1381 VEKWQeecEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14616   155 VRASR---AHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 957-1163 7.87e-28

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: 112.47  E-value: 7.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDD-TEVYGDFKVT 1035
Cdd:cd14635     1 YINAALMD------SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENgVHRHGPIQVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1036 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAGA 1109
Cdd:cd14635    73 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14635   153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1215-1458 1.08e-27

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 115.10  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1215 CSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGeSSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIV 1294
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1295 MLNEV--DLSQGCPQYW--PEEGMLRYGPIQVECMSCSMdcdviNRIFRICNL--TRPQEG-YLMVQQFQYLGWAsHREV 1367
Cdd:PHA02742  123 MITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKIKS-----FRNYAVTNLclTDTNTGaSLDIKHFAYEDWP-HGGL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1368 PGSKRSFLKLILQVEKWQEECE---EGEGRT-----IIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKP 1439
Cdd:PHA02742  197 PRDPNKFLDFVLAVREADLKADvdiKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRH 276

                         250
                  ....*....|....*....
gi 634743231 1440 NMVEAPEQYRFCYDVALEY 1458
Cdd:PHA02742  277 NCLSLPQQYIFCYFIVLIF 295
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1352-1457 1.45e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 108.22  E-value: 1.45e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1352 MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMV-KRQNVVDVFHA 1430
Cdd:smart00404    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 634743231   1431 VKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1352-1457 1.45e-27

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: 108.22  E-value: 1.45e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   1352 MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMV-KRQNVVDVFHA 1430
Cdd:smart00012    1 TVKHYHYTGWPDH-GVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLeAEAGEVDIFDT 78

                            90       100
                    ....*....|....*....|....*..
gi 634743231   1431 VKTLRNSKPNMVEAPEQYRFCYDVALE 1457
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1184-1450 1.81e-27

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: 113.41  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1184 MIRIDSQTNSSHLKDEFQTLNSVTPRLqAEDCsiACLPRNHDKNRFMDMLPPDRCLPFLitidGESSNYINAALMDSyRQ 1263
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGL-AITC--AKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1264 PAAFIVTQY-----PLPNTVKDFWRLVYDYGCTSIVMLNEVDlSQG---CPQYWPE-EGMLRYGPIQVECMScsMDCDvI 1334
Cdd:cd14600    76 PSANIVNKYiatqgPLPHTCAQFWQVVWEQKLSLIVMLTTLT-ERGrtkCHQYWPDpPDVMEYGGFRVQCHS--EDCT-I 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1335 NRIFRICNLTRPQEG-YLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEgegrTIIHCLNGGGRSGMFCAIG 1413
Cdd:cd14600   152 AYVFREMLLTNTQTGeERTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVENEP----VLVHCSAGIGRTGVLVTME 226

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 634743231 1414 IVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRF 1450
Cdd:cd14600   227 TAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1221-1461 1.99e-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: 113.05  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1221 PRNHDKNRFMDMLPPDRCLPFLITIDGE-------SSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSI 1293
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1294 VMLN-EVDLSQG-CPQYWPEEGMLR-YGPIQVECMSCSMDCDVINRIFRICNLTRpQEGYLMVQQFQYLGWASHrEVPGS 1370
Cdd:cd14606    96 VMTTrEVEKGRNkCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVSPLDN-GELIREIWHYQYLSWPDH-GVPSE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1371 KRSFLKLILQVEKWQEECEEGeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNV---VDVFHAVKTLRNSKPNMVEAPEQ 1447
Cdd:cd14606   174 PGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQ 252

                         250
                  ....*....|....
gi 634743231 1448 YRFCYDVALEYLES 1461
Cdd:cd14606   253 YKFIYVAIAQFIET 266
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1252-1453 2.11e-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: 111.32  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAA-FIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLS-QGCPQYWPEE--GMLRYGPIQVECMS 1326
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLvSEQENEkQKVHRYWPTErgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1327 CSMDCDVINRIFRICNltRPQEGYLMVQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRS 1406
Cdd:cd14539    81 VRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 634743231 1407 GMFC-AIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14539   158 GAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1252-1448 2.20e-27

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: 111.07  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLSQGCPQYWP--EEGMLRYGPIQVECMSC 1327
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTrcEEGNRNKCAQYWPsmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1328 SMDCDVINRIFRICNlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecEEGEGRTIIHCLNGGGRSG 1407
Cdd:cd14557    81 KICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 634743231 1408 MFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQY 1448
Cdd:cd14557   156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1252-1459 2.45e-27

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: 110.93  E-value: 2.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALM------DSYRqpaaFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEvDLSQG---CPQYWPE---EGMLRYGP 1319
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQ-DVEGGkvkCHRYWPDslnKPLICGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1320 IQVECMSCSMDCDVINRIFricNLTRPQEGYL-MVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWqeeceEGEGRTIIH 1398
Cdd:cd14538    76 LEVSLEKYQSLQDFVIRRI---SLRDKETGEVhHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRI-----HNSGPIVVH 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1399 CLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYL 1459
Cdd:cd14538   147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 957-1163 9.56e-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: 109.23  E-value: 9.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINAnyidiwLYRDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRV-KCYKYWPDD-TEVYGDFKV 1034
Cdd:cd14637     1 YINA------ALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLAEYVVRTFTLER--RGYNEIREVKQFHFTGW-PDHGVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSAGAG 1110
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1111 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 1163
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 957-1162 3.95e-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: 107.39  E-value: 3.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYkYWPDDTE--VYGDFKV 1034
Cdd:cd17669     1 YINASYIM------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFKV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGA 1109
Cdd:cd17669    74 TLIAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1162
Cdd:cd17669   152 VTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1252-1456 4.35e-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: 107.39  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLSQGCPQYWPEEGMlrygPIQVECMSCSM- 1329
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWPNKDE----PINCETFKVTLi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 --DCDVI----NRIFRICNLTRPQEGYLM-VQQFQYLGWaSHREVPGSKRSFLKLILqvekwQEECEEGEGRTIIHCLNG 1402
Cdd:cd17669    77 aeEHKCLsneeKLIIQDFILEATQDDYVLeVRHFQCPKW-PNPDSPISKTFELISII-----KEEAANRDGPMIVHDEHG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1403 GGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd17669   151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1252-1453 8.84e-26

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: 106.60  E-value: 8.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVdLSQG---CPQYWPEEGMLRYGPIQVECMSCS 1328
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1329 MDCDVINRIFRICNLT--------RPQEgyLMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECEEGEGRTIIHCL 1400
Cdd:cd17668    80 VLAYYTVRNFTLRNTKikkgsqkgRPSG--RVVTQYHYTQWPDM----GVPEYTLPVLTFVRKASYAKRHAVGPVVVHCS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1401 NGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd17668   154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1252-1452 1.71e-25

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 105.62  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALM--DSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQG---CPQYWP-EEGMLR-YGPIQVEC 1324
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaEENESReFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1325 MSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHrEVPGSKRS---FLKLILQVEKwqeeceeGEGRTIIHCLN 1401
Cdd:cd17658    81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDH-GVPKDTRSvreLLKRLYGIPP-------SAGPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1402 GGGRSGMFCAIGIVVEMVKRQNV--VDVFHAVKTLRNSKPNMVEAPEQYRFCY 1452
Cdd:cd17658   153 GIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1221-1459 1.79e-25

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 108.94  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1221 PRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVD 1300
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTK 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1301 LSQG---CPQYW--PEEGMLRYGPIQVECMSCSMDCDVINRIFRICNltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFL 1375
Cdd:PHA02747  129 GTNGeekCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1376 KLILQVEKWQEECEEGEGR-------TIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQY 1448
Cdd:PHA02747  206 KFIKIIDINRKKSGKLFNPkdallcpIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285

                         250
                  ....*....|....
gi 634743231 1449 RF---CYDVALEYL 1459
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1249-1460 3.04e-25

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: 105.41  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1249 SSNYINAALmdsyrqPAAFIVTQY-----PLPNTVKDFWRLVYDYGCTSIVML-NEVDLSQ-GCPQYWPE-EGMLRYGPI 1320
Cdd:cd14601     4 NANYINMEI------PSSSIINRYiacqgPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRvKCHQYWPEpSGSSSYGGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1321 QVECMSCSMDCDVINRIFRICNLTRPQEGYLMvqQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECEEgegRTIIHCL 1400
Cdd:cd14601    78 QVTCHSEEGNPAYVFREMTLTNLEKNESRPLT--QIQYIAWPDH-GVPDDSSDFLDFVCLVRNKRAGKDE---PVVVHCS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1401 NGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLE 1460
Cdd:cd14601   152 AGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1209-1452 4.91e-25

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: 106.20  E-value: 4.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1209 RLQAEDCS--IACLPRNHDKNRFMDMLPPDRCLpflITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVY 1286
Cdd:cd14607     8 RNESHDYPhrVAKYPENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1287 DYGCTSIVMLNEV--DLSQGCPQYWP--EEGMLRYGP--IQVECMSCSMDCDVINRIFRICNLTRPQEgyLMVQQFQYLG 1360
Cdd:cd14607    85 QQKTKAVVMLNRIveKDSVKCAQYWPtdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1361 WASHrEVPGSKRSFLKLILQVEKWQEECEEgEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQN--VVDVFHAVKTLRNSK 1438
Cdd:cd14607   163 WPDF-GVPESPASFLNFLFKVRESGSLSPE-HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYR 240

                         250
                  ....*....|....
gi 634743231 1439 PNMVEAPEQYRFCY 1452
Cdd:cd14607   241 MGLIQTPDQLRFSY 254
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1189-1461 7.20e-25

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 106.33  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1189 SQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPR------NHDKNRFMDMLPPDRclpfliTIDGESSNYINAA---LMD 1259
Cdd:COG5599     2 SPKNPIAIKSEEEKINSRLSTLTNELAPSHNDPQylqninGSPLNRFRDIQPYKE------TALRANLGYLNANyiqVIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1260 SYRqpaaFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLS---QGCPQYWPEEGmlRYGpiQVECMSCSMDCDVIN 1335
Cdd:COG5599    76 NHR----YIATQYPLEEQLEDFFQMLFDNNTPVLVVLaSDDEISkpkVKMPVYFRQDG--EYG--KYEVSSELTESIQLR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1336 R--IFRICNLTRPQEG--YLMVQQFQYLGWASHRevPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCA 1411
Cdd:COG5599   148 DgiEARTYVLTIKGTGqkKIEIPVLHVKNWPDHG--AISAEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIA 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 634743231 1412 IGIVVEMVKRQNV--VDVFHAVKTLRNSK-PNMVEAPEQyrfcYDVALEYLES 1461
Cdd:COG5599   226 CLALSKSINALVQitLSVEEIVIDMRTSRnGGMVQTSEQ----LDVLVKLAEQ 274
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1250-1459 8.22e-25

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: 104.08  E-value: 8.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1250 SNYINAALMDSYRQpaaFIVTQYPLPNTVKDFWRLVYDYGCTSIVML--NEVDLSQGCPQYWP----EEGMLRYGPIQV- 1322
Cdd:cd14540     4 ASHITATVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVtaEEEGGREKCFRYWPtlggEHDALTFGEYKVs 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1323 ECMSCSMDCDVINRiFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLIlqvEKWQE------ECEEGEGR-- 1394
Cdd:cd14540    81 TKFSVSSGCYTTTG-LRVKHTLSGQ--SRTVWHLQYTDWPDH-GCPEDVSGFLDFL---EEINSvrrhtnQDVAGHNRnp 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1395 -TIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYL 1459
Cdd:cd14540   154 pTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1252-1456 2.34e-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: 102.45  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLSQGCPQYWPEegmlrygpiQVECMSC-SM 1329
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQGLAEDEFVYWPS---------REESMNCeAF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1330 DCDVINRIfRIC------------NLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECEEGEGRTI 1396
Cdd:cd17670    72 TVTLISKD-RLClsneeqiiihdfILEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTI 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1397 IHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVAL 1456
Cdd:cd17670   145 VHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 957-1162 5.95e-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: 101.29  E-value: 5.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  957 YINANYIDiwlyrdGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEVYG--DFKV 1034
Cdd:cd17670     1 YINASYIM------GYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPSREESMNceAFTV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1035 TCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHAT-GLLSFIRRVKLSNPpsaGPIVVHCSAG 1108
Cdd:cd17670    74 TLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRD---GPTIVHDEFG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1109 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 1162
Cdd:cd17670   151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1243-1458 5.00e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 102.03  E-value: 5.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1243 ITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLS-QGCPQYW--PEEGMLRYGP 1319
Cdd:PHA02746   91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDdEKCFELWtkEEDSELAFGR 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1320 IQVECMSCSMDCDVINRIFRICNLTrpQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECE-------EGE 1392
Cdd:PHA02746  171 FVAKILDIIEELSFTKTRLMITDKI--SDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAELIkqadndpQTL 247

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1393 GRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYdVALEY 1458
Cdd:PHA02746  248 GPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1252-1460 5.02e-23

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: 98.67  E-value: 5.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1252 YINAA--LMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN-EVDLSQ-GCPQYWPE--EGMLRYGPIQVECM 1325
Cdd:cd14596     1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKvKCHRYWPEtlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1326 SCSMDCDVINRIFRICNltRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEceegeGRTIIHCLNGGGR 1405
Cdd:cd14596    81 NYQALQYFIIRIIKLVE--KETGENRLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAGIGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 634743231 1406 SGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLE 1460
Cdd:cd14596   153 AGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PHA02738 PHA02738
hypothetical protein; Provisional
 1222-1462 5.19e-23

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 101.54  E-value: 5.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1222 RNHDKNRFMDMLPPDRCLPFLITiDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML--NEV 1299
Cdd:PHA02738   48 KNRKLNRYLDAVCFDHSRVILPA-ERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLckKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1300 DLSQGCPQYWP--EEGMLRYGPIQVECMSCSMDCDVINRIFRicnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKL 1377
Cdd:PHA02738  127 NGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLL---LTDGTSATQTVTHFNFTAWPDH-DVPKNTSEFLNF 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1378 ILQVEKWQEECEE-----GEGRT-----IIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQ 1447
Cdd:PHA02738  203 VLEVRQCQKELAQeslqiGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                         250
                  ....*....|....*
gi 634743231 1448 YRFCYDVALEYLESS 1462
Cdd:PHA02738  283 YFFCYRAVKRYVNLT 297
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1223-1459 8.72e-23

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: 98.75  E-value: 8.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1223 NHDKNRFMDMLPPDRCLPFLitidGESSNYINAAL--MDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEV 1299
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1300 DLSQ-GCPQYWPEEgmlRYGPIQVE---CMSCSMDCDVINRIFRICNLTRPQEGYL-MVQQFQYLGWASHrEVPGSKRSF 1374
Cdd:cd14597    79 EGGKiKCQRYWPEI---LGKTTMVDnrlQLTLVRMQQLKNFVIRVLELEDIQTREVrHITHLNFTAWPDH-DTPSQPEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1375 LKLILQVEKWQEEceegeGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDV 1454
Cdd:cd14597   155 LTFISYMRHIHKS-----GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                  ....*
gi 634743231 1455 ALEYL 1459
Cdd:cd14597   230 ILYVL 234
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1216-1460 1.03e-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: 88.13  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1216 SIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAA--FIVTQYPLPNTVKDFWRLVYDYGCTSI 1293
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1294 VMLNeVDLSQGCPQ---YWPEEGMLR----YGPIQVEC-MSCSMDCDVINRIfRICNLTRPQEGylMVQQFQYLGWASH- 1364
Cdd:cd14599   111 AMVT-AEEEGGRSKshrYWPKLGSKHssatYGKFKVTTkFRTDSGCYATTGL-KVKHLLSGQER--TVWHLQYTDWPDHg 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1365 --REVPGSkRSFLKLILQVEKWQEECEEGEGR----TIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSK 1438
Cdd:cd14599   187 cpEEVQGF-LSYLEEIQSVRRHTNSMLDSTKNcnppIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                         250       260
                  ....*....|....*....|..
gi 634743231 1439 PNMVEAPEQYRFCYDVALEYLE 1460
Cdd:cd14599   266 MFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1267-1460 1.17e-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: 74.63  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1267 FIVTQYPLPNTVKDFWRLVYDYGCTSIVMLN--EVDLSQGCPQYWPEEG----MLRYGPIQVECMSCSMDCDVINRIFRI 1340
Cdd:cd14598    18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaeEEGGREKSFRYWPRLGsrhnTVTYGRFKITTRFRTDSGCYATTGLKI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1341 CNLTRPQEgyLMVQQFQYLGWASH---REVPGSkRSFLKLILQVEKWQEECEEGEGRT---IIHCLNGGGRSGMFCAIGI 1414
Cdd:cd14598    98 KHLLTGQE--RTVWHLQYTDWPEHgcpEDLKGF-LSYLEEIQSVRRHTNSTIDPKSPNppvLVHCSAGVGRTGVVILSEI 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 634743231 1415 VVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLE 1460
Cdd:cd14598   175 MIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 884-1161 1.86e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 72.69  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  884 IRVADLLQHInlmkTSDSYGFKEEYESffEGQSASwdvaKKDQNRAKNRYG--NIIAYDHSRVILQPVEDDPSSDYInan 961
Cdd:PHA02740   18 INKPDLLSCI----IKEYRAIVPEHED--EANKAC----AQAENKAKDENLalHITRLLHRRIKLFNDEKVLDARFV--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  962 yidiwlyrDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVgrvKCY-KYWPDD---TEVYGDFKVTCV 1037
Cdd:PHA02740   85 --------DGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCFnQFWSLKegcVITSDKFQIETL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1038 EMEPLAEYVVRTFTLERRgYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV--------KLSNPPSAGPIVVHCSAGA 1109
Cdd:PHA02740  154 EIIIKPHFNLTLLSLTDK-FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIddlcadleKHKADGKIAPIIIDCIDGI 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 634743231 1110 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 1161
Cdd:PHA02740  233 SSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 958-1154 9.21e-13

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: 69.35  E-value: 9.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  958 INANYIDIwlyrdGYQRPShyIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW-PDDTevYGDFKVTc 1036
Cdd:cd14559    18 LNANRVQI-----GNKNVA--IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT--YGSVTVK- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1037 VEMEPLAEYV----VRTFTLERRGYNEIREVKQFHFTGWPDHGvPYHATGLLSFIRRVKLS----------------NPP 1096
Cdd:cd14559    88 SKKTGKDELVdglkADMYNLKITDGNKTITIPVVHVTNWPDHT-AISSEGLKELADLVNKSaeekrnfykskgssaiNDK 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 634743231 1097 SAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIyncVKALR-SRRINMVQTEEQY 1154
Cdd:cd14559   167 NKLLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRtSRNGKMVQKDEQL 222
fn3 pfam00041
Fibronectin type III domain;
488-583 3.95e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.20  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   488 DVPGPVPVKSLQGTSfenkIFLNWKEPLDPNGIITQYEISYSSIRSFDpavpvagPPQTVSNLWNSTHHVFMHLHPGTTY 567
Cdd:pfam00041    1 SAPSNLTVTDVTSTS----LTVSWTPPPDGNGPITGYEVEYRPKNSGE-------PWNEITVPGTTTSVTLTGLKPGTEY 69

                           90
                   ....*....|....*.
gi 634743231   568 QFFIRASTVKGFGPAT 583
Cdd:pfam00041   70 EVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 488-589 1.28e-11

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: 62.13  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  488 DVPGPVPVKSLQGTSfenkIFLNWKEPLDPNGIITQYEISYSSIRSfdpavpvaGPPQTV-SNLWNSTHHVFMHLHPGTT 566
Cdd:cd00063     2 SPPTNLRVTDVTSTS----VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVeVTPGSETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....
gi 634743231  567 YQFFIRASTVKGFG-PATAINVTT 589
Cdd:cd00063    70 YEFRVRAVNGGGESpPSESVTVTT 93
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1066-1159 3.76e-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: 58.13  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1066 FHFTGWPDHGVPyhATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTG----CYIVidIMLDMAEREgvvdiynCVKALR 1141
Cdd:cd14506    79 FYNFGWKDYGVP--SLTTILDIVKVMAFALQEGGKVAVHCHAGLGRTGvliaCYLV--YALRMSADQ-------AIRLVR 147

                          90
                  ....*....|....*...
gi 634743231 1142 SRRINMVQTEEQYIFIHD 1159
Cdd:cd14506   148 SKRPNSIQTRGQVLCVRE 165
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1253-1460 6.29e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 59.21  E-value: 6.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1253 INAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWP--EEGMLRYGPIQVECMscsmd 1330
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFNQFWSlkEGCVITSDKFQIETL----- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1331 cDVINR---IFRICNLTRPQEGYLMVQQFQYLGWA----SHRevPGSKRSFL----KLILQVEKwqEECEEGEGRTIIHC 1399
Cdd:PHA02740  154 -EIIIKphfNLTLLSLTDKFGQAQKISHFQYTAWPadgfSHD--PDAFIDFFcnidDLCADLEK--HKADGKIAPIIIDC 228

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1400 LNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLE 1460
Cdd:PHA02740  229 IDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLK 289
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 492-580 2.97e-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: 52.23  E-value: 2.97e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    492 PVPVKSLQGTSF-ENKIFLNWKEPLDPNGI--ITQYEISYSsirsfdpavPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQ 568
Cdd:smart00060    1 PSPPSNLRVTDVtSTSVTLSWEPPPDDGITgyIVGYRVEYR---------EEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71

                            90
                    ....*....|..
gi 634743231    569 FFIRASTVKGFG 580
Cdd:smart00060   72 FRVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 202-288 5.45e-08

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: 51.74  E-value: 5.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    202 GDVEVNAGQNATFQCIATGRDAVHnkLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSgVS 281
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPE--VTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS-AS 78


                    ....*..
gi 634743231    282 NFAQLIV 288
Cdd:smart00410   79 SGTTLTV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
459-632 5.42e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.16  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  459 PYTNVSLKMILTNPEGRKESEETIIQTDEDVPgPVPVKSLQGTS-FENKIFLNWKEPLDPNgiITQYEISYSSIRSfdpa 537
Cdd:COG3401   201 PGTTYYYRVAATDTGGESAPSNEVSVTTPTTP-PSAPTGLTATAdTPGSVTLSWDPVTESD--ATGYRVYRSNSGD---- 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  538 vpvaGPPQTVSNLwNSTHHVFMHLHPGTTYQFFIRASTVKGF--GPATAINVTTNISAPTLPdyEGVDASlNETATTITv 615
Cdd:COG3401   274 ----GPFTKVATV-TTTSYTDTGLTNGTTYYYRVTAVDAAGNesAPSNVVSVTTDLTPPAAP--SGLTAT-AVGSSSIT- 344

                         170
                  ....*....|....*..
gi 634743231  616 lLRPAQAKGAPISAYQI 632
Cdd:COG3401   345 -LSWTASSDADVTGYNV 360
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1099-1159 5.80e-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: 46.57  E-value: 5.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231 1099 GPIVVHCSAGAGRTGCYIVIDIMLDMaeREGVVDIYNCVKALRSRRINmvQTEEQYIFIHD 1159
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGGIP--QTIEQLDFLIK 113
fn3 pfam00041
Fibronectin type III domain;
294-371 6.26e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   294 PIAPPQLLGVGPTYLLIQLNANSIiGDGPIILKEVEYRMTSGSWTETHAV---NAPTYKLWHLDPDTEYEIRVlLTRPGE 370
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEYRPKNSGEPWNEITvpgTTTSVTLTGLKPGTEYEVRV-QAVNGG 79


                   .
gi 634743231   371 G 371
Cdd:pfam00041   80 G 80
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 206-276 1.52e-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: 44.83  E-value: 1.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 634743231  206 VNAGQNATFQCIATGrDAVHNKLWlqRRNGEDIPVAQTKNINHRrfaASFRLQEVTKTDQDLYRCVTQSER 276
Cdd:cd20957    13 VDFGRTAVFNCSVTG-NPIHTVLW--MKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYQCFVRNDG 77
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1071-1159 3.08e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 45.35  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1071 WPDHGVPyHATGLLSFIRRVKLSNPPSaGPIVVHCSAGAGRTG----CYIVidimldmaeREGvVDIYNCVKALRSRRIN 1146
Cdd:COG2453    55 IPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGtvaaAYLV---------LLG-LSAEEALARVRAARPG 122

                          90
                  ....*....|...
gi 634743231 1147 MVQTEEQYIFIHD 1159
Cdd:COG2453   123 AVETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 292-371 3.10e-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: 3.10e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231    292 PRPIAPPQLLGVGPTYLLIQ-LNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPT-YKLWHLDPDTEYEIRVL-LTRP 368
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsYTLTGLKPGTEYEFRVRaVNGA 80


                    ...
gi 634743231    369 GEG 371
Cdd:smart00060   81 GEG 83
I-set pfam07679
Immunoglobulin I-set domain;
196-288 3.30e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.79  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   196 PHFLR-LGDVEVNAGQNATFQCIATGR---DAVhnklWLqrRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCV 271
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTGTpdpEVS----WF--KDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCV 74

                           90
                   ....*....|....*..
gi 634743231   272 TQSERGSgVSNFAQLIV 288
Cdd:pfam07679   75 ATNSAGE-AEASAELTV 90
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1354-1453 4.12e-05

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: 45.33  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1354 QQFQYLGWASHR------EVPGSKRSFLKLIlqveKWQEECEEGEGRTIIHCLNGGGRSGMFCAigivVEMVKRQNVVDV 1427
Cdd:cd14505    66 EQYQQAGITWHHlpipdgGVPSDIAQWQELL----EELLSALENGKKVLIHCKGGLGRTGLIAA----CLLLELGDTLDP 137

                          90       100
                  ....*....|....*....|....*.
gi 634743231 1428 FHAVKTLRNSKPNMVEAPEQYRFCYD 1453
Cdd:cd14505   138 EQAIAAVRALRPGAIQTPKQENFLHQ 163
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 292-384 4.86e-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: 43.64  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  292 PRPIAPPQLLGVGPTYLLIQLNANSiiGDGPIILK-EVEYR-MTSGSWTE--THAVNAPTYKLWHLDPDTEYEIRVLLTR 367
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPE--DDGGPITGyVVEYReKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....*..
gi 634743231  368 pgEGGTGLPGPPLITRT 384
Cdd:cd00063    79 --GGGESPPSESVTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1267-1448 5.70e-05

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: 46.24  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1267 FIVTQYPLPNTVKDFWRLVYDYGCTSIVML-NEVDLS-QGCPQYWPEEGmlRYGPIQVECMSCSMDCDVINRIFRICNL- 1343
Cdd:cd14559    31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLaSNKDIQrKGLPPYFRQSG--TYGSVTVKSKKTGKDELVDGLKADMYNLk 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231 1344 TRPQEGYLMVQQFQYLGWASHREVPGS---------------KRSFLKLilqvEKWQEECEEGEGRTIIHCLNGGGRSGM 1408
Cdd:cd14559   109 ITDGNKTITIPVVHVTNWPDHTAISSEglkeladlvnksaeeKRNFYKS----KGSSAINDKNKLLPVIHCRAGVGRTGQ 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 634743231 1409 FCAigiVVEMVKRQNVVDVFHAVKTLRNSK-PNMVEAPEQY 1448
Cdd:cd14559   185 LAA---AMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDEQL 222
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1386-1453 9.57e-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: 43.11  E-value: 9.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 634743231 1386 EECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKrqnvvDVFHAVKTLRNSKPNMVEA-PEQYRFCYD 1453
Cdd:cd14494    50 DQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPGGIPQtIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1101-1159 3.40e-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: 3.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634743231 1101 IVVHCSAGAGRTG----CYIvidIMLDM-AEREGVVDIyncVKALRSRRInmvQTEEQYIFIHD 1159
Cdd:cd14505   109 VLIHCKGGLGRTGliaaCLL---LELGDtLDPEQAIAA---VRALRPGAI---QTPKQENFLHQ 163
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 194-288 5.55e-04

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: 40.30  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  194 KSPHflrlgDVEVNAGQNATFQCIATGRDAvhNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQ 273
Cdd:cd05763     4 KTPH-----DITIRAGSTARLECAATGHPT--PQIAWQKDGGTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQ 76

                          90
                  ....*....|....*
gi 634743231  274 SERGSGVSNfAQLIV 288
Cdd:cd05763    77 NSAGSISAN-ATLTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 204-284 7.19e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 39.87  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231   204 VEVNAGQNATFQCIA-TGRDAVHNKLWLQrrNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSN 282
Cdd:pfam00047    6 VTVLEGDSATLTCSAsTGSPGPDVTWSKE--GGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83


                   ..
gi 634743231   283 FA 284
Cdd:pfam00047   84 TS 85
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
478-612 7.38e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.17  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743231  478 SEETIIQTDEDVPGPVPvkSLQGTSFENKIFLNWKEPLDPNgiITQYEISYSSIRSF-DPAVPVAGPPQTvsnlwnstHH 556
Cdd:COG4733   618 SSETTVTGKTAPPPAPT--GLTATGGLGGITLSWSFPVDAD--TLRTEIRYSTTGDWaSATVAQALYPGN--------TY 685

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231  557 VFMHLHPGTTYQFFIRAstVKGFGPATAINVTTNISAPTLPDYEGVDASLNETATT 612
Cdd:COG4733   686 TLAGLKAGQTYYYRARA--VDRSGNVSAWWVSGQASADAAGILDAITGQILETELG 739
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1086-1157 8.68e-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: 8.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634743231 1086 FIRRVKlSNPPSAGPIVVHCSAGAGRTG----CYIVIDIMLDMAEregvvdiynCVKALRSRRINMVQTEEQYIFI 1157
Cdd:cd14504    71 FLDIVE-EANAKNEAVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 203-271 1.62e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 1.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 634743231   203 DVEVNAGQNATFQCIATGRDAVhNKLWLqrRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCV 271
Cdd:pfam13927   10 SVTVREGETVTLTCEATGSPPP-TITWY--KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
 
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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