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Conserved domains on  [gi|57659396|ref|YP_184835|]
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protein-tyrosine phosphatase [Bracoviriform congregatae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-296 0e+00

protein tyrosine phosphatase; Provisional


:

Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    1 MAVNSAVDINGNDFLSFINKPDLLTRIIKEYYALVPKHKEEGNSASAQNENKCKKE-LGMHLTRYLNRRIKLRNDGRVLD 79
Cdd:PHA02740   1 MAIEDAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDEnLALHITRLLHRRIKLFNDEKVLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   80 ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKKCY-QYWSSKEGCVKVSDKFRIKTLKIIIKPH 158
Cdd:PHA02740  81 ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFnQFWSLKEGCVITSDKFQIETLEIIIKPH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  159 FNLTLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTADKKIAPIIVQCLDGISSSAVFCV 238
Cdd:PHA02740 161 FNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIAPIIIDCIDGISSSAVFCV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396  239 FDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVKEKLFMLPFI 296
Cdd:PHA02740 241 FDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILKFI 298
 
Name Accession Description Interval E-value
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-296 0e+00

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    1 MAVNSAVDINGNDFLSFINKPDLLTRIIKEYYALVPKHKEEGNSASAQNENKCKKE-LGMHLTRYLNRRIKLRNDGRVLD 79
Cdd:PHA02740   1 MAIEDAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDEnLALHITRLLHRRIKLFNDEKVLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   80 ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKKCY-QYWSSKEGCVKVSDKFRIKTLKIIIKPH 158
Cdd:PHA02740  81 ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFnQFWSLKEGCVITSDKFQIETLEIIIKPH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  159 FNLTLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTADKKIAPIIVQCLDGISSSAVFCV 238
Cdd:PHA02740 161 FNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIAPIIIDCIDGISSSAVFCV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396  239 FDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVKEKLFMLPFI 296
Cdd:PHA02740 241 FDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILKFI 298
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
68-283 4.28e-44

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 150.89  E-value: 4.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396     68 RIKLRNDGRVLD----ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCV 140
Cdd:smart00194  43 RVKLKPPPGEGSdyinASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKgreKCAQYWPDEEGEP 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    141 KVSDKFRIKTLKIIIKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFycnVKDMclqleRQTADKKI 219
Cdd:smart00194 123 LTYGDITVTLKSVEKVDDYTIRTLEVTNTgCSETRTVTHYHYTNWPDHGVPESPESILDL---IRAV-----RKSQSTST 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57659396    220 APIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKygfMNC---LDDYVLCYQLLA 283
Cdd:smart00194 195 GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR---PGMvqtEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
63-283 7.63e-44

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 149.31  E-value: 7.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    63 RYLN------RRIKLRNDGRVLD---ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCY 130
Cdd:pfam00102   6 RYKDvlpydhTRVKLTGDPGPSDyinASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKgreKCA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   131 QYWSSKEGCVKVSDKFRIKTLKI-IIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCL 208
Cdd:pfam00102  86 QYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEEtRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396   209 QLERqtadkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLA 283
Cdd:pfam00102 166 DGRS-------GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 80-280 2.05e-42

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: 144.74  E-value: 2.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  80 ASFVDGYDFERKYICIkrlQ---EDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSDKFRIKTLKI 153
Cdd:cd00047   4 ASYIDGYRGPKEYIAT---QgplPNTVEDFWRMVWEQKVSVIVMLTNLVEKgreKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 154 IIKPHFNLTLLSLT-DKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkdmclqleRQTADKKIAPIIVQCLDGISS 232
Cdd:cd00047  81 EELSDYTIRTLELSpKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRV--------RKEARKPNGPIVVHCSAGVGR 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 57659396 233 SAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd00047 153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
 
Name Accession Description Interval E-value
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-296 0e+00

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 549.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    1 MAVNSAVDINGNDFLSFINKPDLLTRIIKEYYALVPKHKEEGNSASAQNENKCKKE-LGMHLTRYLNRRIKLRNDGRVLD 79
Cdd:PHA02740   1 MAIEDAVDINGMDFINFINKPDLLSCIIKEYRAIVPEHEDEANKACAQAENKAKDEnLALHITRLLHRRIKLFNDEKVLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   80 ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKKCY-QYWSSKEGCVKVSDKFRIKTLKIIIKPH 158
Cdd:PHA02740  81 ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCFnQFWSLKEGCVITSDKFQIETLEIIIKPH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  159 FNLTLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTADKKIAPIIVQCLDGISSSAVFCV 238
Cdd:PHA02740 161 FNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIAPIIIDCIDGISSSAVFCV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396  239 FDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVKEKLFMLPFI 296
Cdd:PHA02740 241 FDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILKFI 298
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
68-283 4.28e-44

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 150.89  E-value: 4.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396     68 RIKLRNDGRVLD----ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCV 140
Cdd:smart00194  43 RVKLKPPPGEGSdyinASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKgreKCAQYWPDEEGEP 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    141 KVSDKFRIKTLKIIIKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFycnVKDMclqleRQTADKKI 219
Cdd:smart00194 123 LTYGDITVTLKSVEKVDDYTIRTLEVTNTgCSETRTVTHYHYTNWPDHGVPESPESILDL---IRAV-----RKSQSTST 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57659396    220 APIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKygfMNC---LDDYVLCYQLLA 283
Cdd:smart00194 195 GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQR---PGMvqtEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
63-283 7.63e-44

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 149.31  E-value: 7.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    63 RYLN------RRIKLRNDGRVLD---ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCY 130
Cdd:pfam00102   6 RYKDvlpydhTRVKLTGDPGPSDyinASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKgreKCA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   131 QYWSSKEGCVKVSDKFRIKTLKI-IIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCL 208
Cdd:pfam00102  86 QYWPEEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEEtRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRKSSL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396   209 QLERqtadkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLA 283
Cdd:pfam00102 166 DGRS-------GPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 8-286 4.59e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 150.08  E-value: 4.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    8 DINGNDFLSFINKPDLLTRIIKEYYALVPKHKEEGNSASAQNENkckkelgmhLTRYLN------RRIKL---RNDGRVL 78
Cdd:PHA02738   8 ELKYAEFLALMEKSDCEEVITREHQKVISEKVDGTFNAEKKNRK---------LNRYLDavcfdhSRVILpaeRNRGDYI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   79 DASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGCVKVSDKFRIKTLKIII 155
Cdd:PHA02738  79 NANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEngrEKCFPYWSDVEQGSIRFGKFKITTTQVET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  156 KPHFNLTLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLER---QTADKKIA--PIIVQCLDGI 230
Cdd:PHA02738 159 HPHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQeslQIGHNRLQppPIVVHCNAGL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 57659396  231 SSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYV 286
Cdd:PHA02738 239 GRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYV 294
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 80-280 2.05e-42

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: 144.74  E-value: 2.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  80 ASFVDGYDFERKYICIkrlQ---EDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSDKFRIKTLKI 153
Cdd:cd00047   4 ASYIDGYRGPKEYIAT---QgplPNTVEDFWRMVWEQKVSVIVMLTNLVEKgreKCERYWPEEGGKPLEYGDITVTLVSE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 154 IIKPHFNLTLLSLT-DKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkdmclqleRQTADKKIAPIIVQCLDGISS 232
Cdd:cd00047  81 EELSDYTIRTLELSpKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRV--------RKEARKPNGPIVVHCSAGVGR 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 57659396 233 SAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd00047 153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1-277 2.32e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 145.14  E-value: 2.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    1 MAVNSAVDINGNDFLSFINKPDLLTRIIKEYYALV--PKHKEEGNSASAQNENKckkelgmhlTRYLN------RRIKLR 72
Cdd:PHA02747   1 MDSNCFAECRAIDFLKRRNQLNCFGIIRDEHHQIIlkPFDGLIANFEKPENQPK---------NRYWDipcwdhNRVILD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   73 NDG----RVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLS----DKKCYQYWSSKEGCVKVSD 144
Cdd:PHA02747  72 SGGgstsDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKgtngEEKCYQYWCLNEDGNIDME 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  145 KFRIKTLKIIIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNfshKPDAFIDF--YCNVKDMCLQLERQTADKK--- 218
Cdd:PHA02747 152 DFRIETLKTSVRAKYILTLIEITDKILKDsRKISHFQCSEWFEDE---TPSDHPDFikFIKIIDINRKKSGKLFNPKdal 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 57659396  219 IAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVL 277
Cdd:PHA02747 229 LCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 78-287 1.87e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 142.45  E-value: 1.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSDKFRIKTLKII 154
Cdd:PHA02742  81 INASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDgkeACYPYWMPHERGKATHGEFKIKTKKIK 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  155 IKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTADKKI---APIIVQCLDGI 230
Cdd:PHA02742 161 SFRNYAVTNLCLTDTnTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGENIvkePPILVHCSAGL 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 57659396  231 SSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:PHA02742 241 DRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 73-282 5.48e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 120.90  E-value: 5.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396   73 NDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRL--SDKKCYQYWSSKEGCVKVSDKFRIKT 150
Cdd:PHA02746  96 NAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIddDDEKCFELWTKEEDSELAFGRFVAKI 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  151 LKIIIKPHFNLTLLSLTDKFGQ-EQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTAD--KKIAPIIVQCL 227
Cdd:PHA02746 176 LDIIEELSFTKTRLMITDKISDtSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADNdpQTLGPIVVHCS 255

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 57659396  228 DGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:PHA02746 256 AGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 27-279 2.53e-29

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: 112.46  E-value: 2.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  27 IIKEYYALVPKHKEEGNSASAQNENKCKkelgmhlTRYLN------RRIKLRNDGR-----VLDASFVDGYDFERKYICI 95
Cdd:cd14543   5 IYEEYEDIRREPPAGTFLCSLAPANQEK-------NRYGDvlcldqSRVKLPKRNGdertdYINANFMDGYKQKNAYIAT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  96 KRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGCVKVSDKFRIKTLKIIIKPHFNLTLLSLTDKFGQ 172
Cdd:cd14543  78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVErgrVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 173 EQK-ISHYQYTAWPGDNFSHKPDAFIDFYCNVK----DMCLQL-ERQTADKKIAPIIVQCLDGISSSAVFCVFDICATQF 246
Cdd:cd14543 158 ESRqVTHFQFTSWPDFGVPSSAAALLDFLGEVRqqqaLAVKAMgDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQL 237

                       250       260       270
                ....*....|....*....|....*....|...
gi 57659396 247 DKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14543 238 EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 68-280 1.75e-27

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: 106.32  E-value: 1.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  68 RIKL-RNDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEG---CV 140
Cdd:cd14545  16 RVKLkQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKgqiKCAQYWPQGEGnamIF 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 141 KvSDKFRIKTLKIIIKPHFNLTLLSLTDKFGQEQK-ISHYQYTAWPGDNFSHKPDAFIDFycnvkdmcLQLERQTA--DK 217
Cdd:cd14545  96 E-DTGLKVTLLSEEDKSYYTVRTLELENLKTQETReVLHFHYTTWPDFGVPESPAAFLNF--------LQKVRESGslSS 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 218 KIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLS--LPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14545 167 DVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSvdVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 68-292 2.95e-25

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: 101.64  E-value: 2.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  68 RIKL-RNDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVS 143
Cdd:cd14608  41 RIKLhQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKgslKCAQYWPQKEEKEMIF 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 144 D--KFRIKTLKIIIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlERQTADKKIA 220
Cdd:cd14608 121 EdtNLKLTLISEDIKSYYTVRQLELENLTTQEtREILHFHYTTWPDFGVPESPASFLNFLFKVR------ESGSLSPEHG 194

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 221 PIIVQCLDGISSSAVFCVFDICATQFDK---TGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYqlLAVYVKEKLFM 292
Cdd:cd14608 195 PVVVHCSAGIGRSGTFCLADTCLLLMDKrkdPSSVDIKKVLLEMRKFRMGLIQTADQLRFSY--LAVIEGAKFIM 267
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 64-279 1.45e-24

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 99.27  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  64 YLNRRIKLRN-DGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGC 139
Cdd:cd14607  36 YDHSRVKLQNtENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKdsvKCAQYWPTDEEE 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 140 VKV--SDKFRIKTLKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDM-CLQLERqta 215
Cdd:cd14607 116 VLSfkETGFSVKLLSEDVKSYYTVHLLQLENiNSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgSLSPEH--- 192

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57659396 216 dkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLS--LPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14607 193 ----GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSvdIKQVLLDMRKYRMGLIQTPDQLRFSY 254
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 51-280 3.42e-24

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: 97.98  E-value: 3.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  51 NKCKKELgMHLTRYLNRRIKLRN----DGR-VLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLS 125
Cdd:cd14554   6 NKFKNRL-VNILPYESTRVCLQPirgvEGSdYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 126 D---KKCYQYWSSKEGcVKVSdKFRIKTLKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYC 201
Cdd:cd14554  85 EmgrEKCHQYWPAERS-ARYQ-YFVVDPMAEYNMPQYILREFKVTDaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57659396 202 NVKDMCLQLERQtadkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14554 163 QVHKTKEQFGQE------GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 50-286 8.86e-23

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: 95.18  E-value: 8.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  50 ENKCKKELGMHLTRYLNRRIKLRNDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD--- 126
Cdd:cd14629  56 KNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmgr 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 127 KKCYQYWSSKEGCvkVSDKFRIKTLKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKD 205
Cdd:cd14629 136 EKCHQYWPAERSA--RYQYFVVDPMAEYNMPQYILREFKVTDaRDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHK 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 206 MCLQLERQtadkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVY 285
Cdd:cd14629 214 TKEQFGQD------GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287


                .
gi 57659396 286 V 286
Cdd:cd14629 288 L 288
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 78-286 1.49e-21

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: 92.10  E-value: 1.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGCVkvSDKFRIKTLKII 154
Cdd:cd14627  84 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREmgrEKCHQYWPAERSAR--YQYFVVDPMAEY 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQtadkkiAPIIVQCLDGISSS 233
Cdd:cd14627 162 NMPQYILREFKVTDaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQD------GPISVHCSAGVGRT 235

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYV 286
Cdd:cd14627 236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 87-286 2.15e-20

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: 87.13  E-value: 2.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  87 DFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLIS---RLSDKKCYQYW--SSKEGCVKVSDKFRIKTLKIIIKPHFNL 161
Cdd:cd14540  13 GKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTaeeEGGREKCFRYWptLGGEHDALTFGEYKVSTKFSVSSGCYTT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 162 TLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQL-ERQTADKKIAPIIVQCLDGISSSAVFCVF 239
Cdd:cd14540  93 TGLRVKHtLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTnQDVAGHNRNPPTLVHCSAGVGRTGVVILA 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 57659396 240 DICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYV 286
Cdd:cd14540 173 DLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 66-267 2.40e-20

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: 87.07  E-value: 2.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  66 NRRIKLRN-----DGRVLDASFVDGYDFERK-YICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK--KCYQYWSSKE 137
Cdd:cd14547  11 HSRVCLPSvdddpLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAkeKCAQYWPEEE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 138 GcvKVSDKFRIKTLKIIIKPHFNLTLLSLTDKfGQEQKISHYQYTAWPGDNFSHKPDAFIDfycnvkdmcLQLERQTADK 217
Cdd:cd14547  91 N--ETYGDFEVTVQSVKETDGYTVRKLTLKYG-GEKRYLKHYWYTSWPDHKTPEAAQPLLS---------LVQEVEEARQ 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57659396 218 KIA---PIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYG 267
Cdd:cd14547 159 TEPhrgPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGG 211
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 78-279 2.91e-20

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: 86.29  E-value: 2.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKR-LQEDACDkFWQAVSNYKVQIIVLISRLSDKK---CYQYWSSK-------EGCVKVSDKF 146
Cdd:cd14558   2 INASFIDGYWGPKSLIATQGpLPDTIAD-FWQMIFQKKVKVIVMLTELKEGDqeqCAQYWGDEkktygdiEVELKDTEKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 147 RIKTLKiiikpHFNLTLLSLTDkfgqEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTAdkKIAPIIVQC 226
Cdd:cd14558  81 PTYTVR-----VFEITHLKRKD----SRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHG--RSVPIVVHC 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57659396 227 LDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14558 150 SDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 78-286 1.05e-19

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: 86.71  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGCvkVSDKFRIKTLKII 154
Cdd:cd14628  83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmgrEKCHQYWPAERSA--RYQYFVVDPMAEY 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQtadkkiAPIIVQCLDGISSS 233
Cdd:cd14628 161 NMPQYILREFKVTDaRDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQD------GPISVHCSAGVGRT 234

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYV 286
Cdd:cd14628 235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 89-282 2.37e-19

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: 84.03  E-value: 2.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  89 ERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSDKFRIKTLKIIIKPHFNLTLLS 165
Cdd:cd14596  15 ELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERgkvKCHRYWPETLQEPMELENYQLRLENYQALQYFIIRIIK 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 166 LTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQlerqtadkkiAPIIVQCLDGISSSAVFCVFDICAT 244
Cdd:cd14596  95 LVEKeTGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----------GPIVVHCSAGIGRAGVLICVDVLLS 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 57659396 245 QFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14596 165 LIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 78-282 5.72e-19

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: 83.10  E-value: 5.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYW----SSKEGCVKVSDKfRIKT 150
Cdd:cd17668   2 INANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCDQYWpadgSEEYGNFLVTQK-SVQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 151 LKIIIKPHFnlTLLSLTDKFG------QEQKISHYQYTAWPGDNFSHKPDAFIDFycnvkdmcLQLERQTADKKIAPIIV 224
Cdd:cd17668  81 LAYYTVRNF--TLRNTKIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTF--------VRKASYAKRHAVGPVVV 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396 225 QCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd17668 151 HCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 92-282 1.51e-18

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: 82.04  E-value: 1.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  92 YICIKRLQEDACDKFWQAVSNYKVQIIVLISR--LSDK-KCYQYW-SSKEGCVKVSDKFRIKTLKIIIKPHFNLTLLSLT 167
Cdd:cd14538  18 YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQdvEGGKvKCHRYWpDSLNKPLICGGRLEVSLEKYQSLQDFVIRRISLR 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 168 DK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCnvkdmclqLERQTADKkiAPIIVQCLDGISSSAVFCVFDICATQF 246
Cdd:cd14538  98 DKeTGEVHHITHLNFTTWPDHGTPQSADPLLRFIR--------YMRRIHNS--GPIVVHCSAGIGRTGVLITIDVALGLI 167

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 57659396 247 DKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14538 168 ERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 65-285 2.07e-18

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: 82.58  E-value: 2.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  65 LNRRIKLRNDGRVLDASFVDGYD-FERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK--KCYQYWSSKEGCVk 141
Cdd:cd14612  34 LRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEKkeKCVHYWPEKEGTY- 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 142 vsDKFRIKTLKIiiKPHFNLTLLSLTDKFGQEQK-ISHYQYTAWPGDNFSHKPDAFIDFYCNVKDmclqlERQTADKKiA 220
Cdd:cd14612 113 --GRFEIRVQDM--KECDGYTIRDLTIQLEEESRsVKHYWFSSWPDHQTPESAGPLLRLVAEVEE-----SRQTAASP-G 182

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 221 PIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVY 285
Cdd:cd14612 183 PIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTLALY 247
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 78-285 8.83e-18

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: 81.06  E-value: 8.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERK-YICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK--KCYQYWSSKEGcvkVSDKFRIKTLKII 154
Cdd:cd14613  57 INANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEMneKCTEYWPEEQV---TYEGIEITVKQVI 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTdKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDmclqlERQTADKKIAPIIVQCLDGISSSA 234
Cdd:cd14613 134 HADDYRLRLITLK-SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEE-----ARQQAEPNCGPVIVHCSAGIGRTG 207

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 57659396 235 VFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVY 285
Cdd:cd14613 208 CFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVLSLY 258
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 78-280 2.44e-17

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: 78.33  E-value: 2.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGCVKVSDKFRIKTLKII 154
Cdd:cd14557   2 INASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEgnrNKCAQYWPSMEEGSRAFGDVVVKINEEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTDK--FGQEQKISHYQYTAWPGDNFSHKPdafidfycnvkDMCLQLERQTADKKIA---PIIVQCLDG 229
Cdd:cd14557  82 ICPDYIIRKLNINNKkeKGSGREVTHIQFTSWPDHGVPEDP-----------HLLLKLRRRVNAFNNFfsgPIVVHCSAG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 57659396 230 ISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14557 151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 64-287 6.47e-17

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: 78.27  E-value: 6.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  64 YLNRR-IKLRNDGRVLDASfvdgydfERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGC 139
Cdd:cd14544  32 YINANyIRNENEGPTTDEN-------AKTYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERgknKCVRYWPD-EGM 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 140 VKVSDKFRIKTLKIIIKPHFNLTLLSLT--DKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlERQTADK 217
Cdd:cd14544 104 QKQYGPYRVQNVSEHDTTDYTLRELQVSklDQGDPIREIWHYQYLSWPDHGVPSDPGGVLNFLEDVN------QRQESLP 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57659396 218 KIAPIIVQCLDGISSSAVFCVFDICATQFDKTG---TLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:cd14544 178 HAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 78-282 7.92e-17

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: 77.31  E-value: 7.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGCVKVSDkFRIKTLKII 154
Cdd:cd14552   2 INASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERsqnKCAQYWPE-DGSVSSGD-ITVELKDQT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNL-TLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDfycnvkdMCLQLERQTADKKIAPIIVQCLDGISSS 233
Cdd:cd14552  80 DYEDYTLrDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMID-------LIAAVQKQQQQSGNHPITVHCSAGAGRT 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14552 153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
175-283 1.16e-16

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 73.93  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    175 KISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTadkkiaPIIVQCLDGISSSAVFCVFDICATQFDK-TGTLS 253
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSG------PVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 57659396    254 LPSVLKKVRQQKYGFMNCLDDYVLCYQLLA 283
Cdd:smart00404  75 IFDTVKELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 175-283 1.16e-16

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 73.93  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396    175 KISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTadkkiaPIIVQCLDGISSSAVFCVFDICATQFDK-TGTLS 253
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSG------PVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 57659396    254 LPSVLKKVRQQKYGFMNCLDDYVLCYQLLA 283
Cdd:smart00012  75 IFDTVKELRSQRPGMVQTEEQYLFLYRALL 104
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 68-285 2.75e-16

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: 76.81  E-value: 2.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  68 RIKLRNDGRVLDASFVD----GYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGcV 140
Cdd:cd14600  56 RVVLQGNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERgrtKCHQYWPDPPD-V 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 141 KVSDKFRI--KTLKIIIKPHFNLTLLSLTdKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLErqtadkk 218
Cdd:cd14600 135 MEYGGFRVqcHSEDCTIAYVFREMLLTNT-QTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE------- 206

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396 219 iaPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDY-VLCYQLLAVY 285
Cdd:cd14600 207 --PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYkFVCEAILRVY 272
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 50-286 2.86e-16

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: 76.41  E-value: 2.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  50 ENKcKKELGMHLTRYLNRRIKLRNDGRVLDASFVD---GyDFERKYI-CIKRLQEDACDkFWQAVSNYKVQIIVLISRLS 125
Cdd:cd14597   2 ENR-KKNRYKNILPYDTTRVPLGDEGGYINASFIKmpvG-DEEFVYIaCQGPLPTTVAD-FWQMVWEQKSTVIAMMTQEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 126 DK---KCYQYWSSKEG-CVKVSDKFRIKTLKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFY 200
Cdd:cd14597  79 EGgkiKCQRYWPEILGkTTMVDNRLQLTLVRMQQLKNFVIRVLELEDiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 201 CNVKDMclqlerqtadKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14597 159 SYMRHI----------HKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                ....*.
gi 57659396 281 LLaVYV 286
Cdd:cd14597 229 VI-LYV 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 78-240 7.68e-16

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: 75.63  E-value: 7.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISR---LSDKKCYQYWSSKEGCVKVSdKFRIKTLKII 154
Cdd:cd14603  61 INANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACReieMGKKKCERYWAQEQEPLQTG-PFTITLVKEK 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 iKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNFSHKPDAFIDFycnvkdmcLQLERQTADKKIAPIIVQCLDGISSS 233
Cdd:cd14603 140 -RLNEEVILRTLKVTFQKEsRSVSHFQYMAWPDHGIPDSPDCMLAM--------IELARRLQGSGPEPLCVHCSAGCGRT 210


                ....*..
gi 57659396 234 AVFCVFD 240
Cdd:cd14603 211 GVICTVD 217
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 78-280 2.67e-15

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: 72.83  E-value: 2.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLS--DKKCYQYWSSKEGcvKVSDKFRIKTLKIII 155
Cdd:cd14556   2 INAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDpkDQSCPQYWPDEGS--GTYGPIQVEFVSTTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 156 KPHFNLTLLSLTDKF-GQEQK--ISHYQYTAWPGDNFShkPDAFIDFYcnvkDMCLQLERQTADKKIAPIIVQCLDGISS 232
Cdd:cd14556  80 DEDVISRIFRLQNTTrPQEGYrmVQQFQFLGWPRDRDT--PPSKRALL----KLLSEVEKWQEQSGEGPIVVHCLNGVGR 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 57659396 233 SAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14556 154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 64-280 3.44e-15

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: 73.16  E-value: 3.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  64 YLNRRIKLRNDGRV-----LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSS 135
Cdd:cd14548   8 YDHSRVKLIPINEEegsdyINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgrvKCDHYWPF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 136 KEGCVKVSDkFRIKTLKIIIKPHFNLTLLSLTDKfGQEQKISHYQYTAWPGDNFSHKPDAFIDFycnvkdmcLQLERQTA 215
Cdd:cd14548  88 DQDPVYYGD-ITVTMLSESVLPDWTIREFKLERG-DEVRSVRQFHFTAWPDHGVPEAPDSLLRF--------VRLVRDYI 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 216 DKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14548 158 KQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 78-282 6.89e-15

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: 72.38  E-value: 6.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGCVKVSDkFRIKTLKII 154
Cdd:cd14623  27 VNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgqeKCAQYWPS-DGSVSYGD-ITIELKKEE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNL-TLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkdmclqlERQTADKKIAPIIVQCLDGISSS 233
Cdd:cd14623 105 ECESYTVrDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAV-------QKQQQQSGNHPITVHCSAGAGRT 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14623 178 GTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 89-287 6.94e-15

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: 72.74  E-value: 6.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  89 ERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGCVKVSDKFRIKTLKIIIKPHFNLTLLS 165
Cdd:cd14605  53 KKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERgksKCVKYWPD-EYALKEYGVMRVRNVKESAAHDYILRELK 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 166 LTdKFGQ---EQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlERQTADKKIAPIIVQCLDGISSSAVFCVFDIC 242
Cdd:cd14605 132 LS-KVGQgntERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVH------HKQESIMDAGPVVVHCSAGIGRTGTFIVIDIL 204

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 57659396 243 ATQFDKTGT---LSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:cd14605 205 IDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIE 252
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 78-275 8.55e-15

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: 71.87  E-value: 8.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGY-DFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK--KCYQYWSSKEGCVKvsdkfRIKTLKII 154
Cdd:cd14611  31 INANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKneKCVLYWPEKRGIYG-----KVEVLVNS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTDKFG-QEQKISHYQYTAWPgdnfSHK-PDAFIDFYCNVKDmcLQLERQTADKKiAPIIVQCLDGISS 232
Cdd:cd14611 106 VKECDNYTIRNLTLKQGsQSRSVKHYWYTSWP----DHKtPDSAQPLLQLMLD--VEEDRLASPGR-GPVVVHCSAGIGR 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 57659396 233 SAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDY 275
Cdd:cd14611 179 TGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQY 221
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 78-272 1.19e-14

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: 71.66  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIK-RLQEDACDkFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKE----GCVKVSdkfrik 149
Cdd:cd14553  34 INANYCDGYRKQNAYIATQgPLPETFGD-FWRMVWEQRSATIVMMTKLEERsrvKCDQYWPTRGtetyGLIQVT------ 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 150 TLKIIIKPHFNLTLLSLTdKFGQEQK--ISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMClqlerqTADKkiAPIIVQCL 227
Cdd:cd14553 107 LLDTVELATYTVRTFALH-KNGSSEKreVRQFQFTAWPDHGVPEHPTPFLAFLRRVKACN------PPDA--GPIVVHCS 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 57659396 228 DGISSSAVFCVFDicatqfdktgtlslpSVLKKVRQQK----YGFMNCL 272
Cdd:cd14553 178 AGVGRTGCFIVID---------------SMLERIKHEKtvdiYGHVTCL 211
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 87-287 1.37e-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: 71.16  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  87 DFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYW--------SSKEGCVKVSDKFRIK-----T 150
Cdd:cd14598  13 GKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEggrEKSFRYWprlgsrhnTVTYGRFKITTRFRTDsgcyaT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 151 LKIIIKphfnlTLLSltdkfGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMcLQLERQTADKKIA--PIIVQCLD 228
Cdd:cd14598  93 TGLKIK-----HLLT-----GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSV-RRHTNSTIDPKSPnpPVLVHCSA 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57659396 229 GISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:cd14598 162 GVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 60-282 1.71e-14

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: 71.99  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  60 HLTRYLN------RRIKLR----NDGR---VLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD 126
Cdd:cd17667  29 HKNRYINilaydhSRVKLRplpgKDSKhsdYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 127 K---KCYQYWSSKEgcvkvSDKFR--IKTLKiIIKPHFNLTLLSLT-----DKFGQ---------EQKISHYQYTAWPGD 187
Cdd:cd17667 109 KgrrKCDQYWPTEN-----SEEYGniIVTLK-STKIHACYTVRRFSirntkVKKGQkgnpkgrqnERTVIQYHYTQWPDM 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 188 NFSHKPDAFIDFycnvkdmclqLERQTADK--KIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQK 265
Cdd:cd17667 183 GVPEYALPVLTF----------VRRSSAARtpEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 252

                       250
                ....*....|....*..
gi 57659396 266 YGFMNCLDDYVLCYQLL 282
Cdd:cd17667 253 NYLVQTEEQYIFIHDAL 269
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 78-280 1.78e-14

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: 70.71  E-value: 1.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWsSKEGCVKVSD-KFRIK-TLK 152
Cdd:cd14551   2 INASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkeKKCSQYW-PDQGCWTYGNlRVRVEdTVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 153 IIIKPHFNLTLLSLTDKFGQE--QKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERqtadkkiaPIIVQCLDGI 230
Cdd:cd14551  81 LVDYTTRKFCIQKVNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAG--------PIVVHCSAGV 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 57659396 231 SSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14551 153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 78-279 1.95e-14

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: 70.46  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEgcVKVSDKFRIKTLKII 154
Cdd:cd14549   2 INANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgrrKCDQYWPKEG--TETYGNIQVTLLSTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSL-------TDKFGQEQKISHYQYTAWPgdnfSHK-PDafidFYCNVkdmcLQLERQTADKK---IAPII 223
Cdd:cd14549  80 VLATYTVRTFSLknlklkkVKGRSSERVVYQYHYTQWP----DHGvPD----YTLPV----LSFVRKSSAANppgAGPIV 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 57659396 224 VQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14549 148 VHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 78-285 3.67e-14

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: 69.65  E-value: 3.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGCVKVSDkfriktLKII 154
Cdd:cd14622   3 INASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReqeKCVQYWPS-EGSVTHGE------ITIE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTD---KFGQEQK---ISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclQLERQTADKkiaPIIVQCLD 228
Cdd:cd14622  76 IKNDTLLETISIRDflvTYNQEKQtrlVRQFHFHGWPEIGIPAEGKGMIDLIAAVQ----KQQQQTGNH---PIVVHCSA 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57659396 229 GISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVY 285
Cdd:cd14622 149 GAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 78-282 1.20e-13

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: 68.81  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSK----EGCVKVSDK----- 145
Cdd:cd14620  26 INASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERkeeKCYQYWPDQgcwtYGNIRVAVEdcvvl 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 146 --FRIKtlKIIIKPHfnltllsLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMclqlerqtADKKIAPII 223
Cdd:cd14620 106 vdYTIR--KFCIQPQ-------LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV--------NPVHAGPIV 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57659396 224 VQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14620 169 VHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 26-282 1.88e-13

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: 68.97  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  26 RIIKEYYALVPKHK---EEGNSASAQNENKCKKELGMHLTRYLNRRIKLRNDGRVLDASFVDGYDFERKYICIKRLQEDA 102
Cdd:cd14625  23 KLSQEYESIDPGQQftwEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPET 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 103 CDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEgcVKVSDKFRIKTLKIIIKPHFNLTLLSLTDKFGQEQK-ISH 178
Cdd:cd14625 103 FGDFWRMVWEQRSATVVMMTKLEEKsriKCDQYWPSRG--TETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKReVRQ 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 179 YQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerqTADKKIA-PIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSV 257
Cdd:cd14625 181 FQFTAWPDHGVPEYPTPFLAFLRRVK---------TCNPPDAgPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGH 251

                       250       260
                ....*....|....*....|....*
gi 57659396 258 LKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14625 252 VTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 78-280 2.49e-13

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: 67.45  E-value: 2.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISR---LSDKKCYQYWSSKEG-----------CVK-- 141
Cdd:cd14542   2 INANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACRefeMGKKKCERYWPEEGEeqlqfgpfkisLEKek 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 142 -VSDKFRIKTLKIiikphfnltllsltdKFGQEQK-ISHYQYTAWPGDNFSHKPDAFIDFycnvkdmcLQLERQTADKKI 219
Cdd:cd14542  82 rVGPDFLIRTLKV---------------TFQKESRtVYQFHYTAWPDHGVPSSVDPILDL--------VRLVRDYQGSED 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 220 APIIVQCLDGISSSAVFCVFDIcATQFDKTGTL----SLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14542 139 VPICVHCSAGCGRTGTICAIDY-VWNLLKTGKIpeefSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 29-282 2.96e-13

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: 68.60  E-value: 2.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  29 KEYYALVPKHK---EEGNSASAQNENKCKKELGMHLTRYLNRRIKLRNDGRVLDASFVDGYDFERKYICIKRLQEDACDK 105
Cdd:cd14624  26 QEYESIDPGQQftwEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGD 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 106 FWQAVSNYKVQIIVLISRLSDK---KCYQYWSSK----EGCVKVS--DKFRIKTLKIiikphfnLTLLSLTDKFGQEQKI 176
Cdd:cd14624 106 FWRMIWEQRSATVVMMTKLEERsrvKCDQYWPSRgtetYGLIQVTllDTVELATYCV-------RTFALYKNGSSEKREV 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 177 SHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPS 256
Cdd:cd14624 179 RQFQFTAWPDHGVPEHPTPFLAFLRRVK--------TCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYG 250

                       250       260
                ....*....|....*....|....*.
gi 57659396 257 VLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14624 251 HVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 26-282 4.30e-13

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: 68.13  E-value: 4.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  26 RIIKEYYALVPKHKEEGNSASAQNENKCKKELGMHLTRYLNRRIKLRN-----DGRVLDASFVDGYDFERKYICIKRLQE 100
Cdd:cd14621  26 KLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPvegvpDSDYINASFINGYQEKNKFIAAQGPKE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 101 DACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGC-----VKVSDKFRIKTLKIIIKPHFNLTLLSLTDKFGQ 172
Cdd:cd14621 106 ETVNDFWRMIWEQNTATIVMVTNLKERkecKCAQYWPD-QGCwtygnIRVSVEDVTVLVDYTVRKFCIQQVGDVTNKKPQ 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 173 eQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLErqtadkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTL 252
Cdd:cd14621 185 -RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--------GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKV 255

                       250       260       270
                ....*....|....*....|....*....|
gi 57659396 253 SLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14621 256 DVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 78-236 5.80e-13

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: 66.58  E-value: 5.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVD----GYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSkEGCVKVSDKFRIKT 150
Cdd:cd14541   3 INANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERgrvKCHQYWPD-LGETMQFGNLQITC 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 151 LKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkdmclqleRQTADKKIAPIIVQCLDG 229
Cdd:cd14541  82 VSEEVTPSFAFREFILTNtNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV--------RQNRVGMVEPTVVHCSAG 153


                ....*..
gi 57659396 230 ISSSAVF 236
Cdd:cd14541 154 IGRTGVL 160
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 103-280 7.19e-13

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: 66.25  E-value: 7.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 103 CDKFWQAVSNYKVQIIVLI---SRLSDKKCYQYWSSKEGCVKVSDKFRI-----KTLKIIIKPHFNLTllSLTDKfgQEQ 174
Cdd:cd14539  28 AADFWLMVYEQQVSVIVMLvseQENEKQKVHRYWPTERGQALVYGAITVslqsvRTTPTHVERIISIQ--HKDTR--LSR 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 175 KISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMcLQLERQTAdkkiAPIIVQCLDGISSSAVFC-----VFDICATQfdkt 249
Cdd:cd14539 104 SVVHLQFTTWPELGLPDSPNPLLRFIEEVHSH-YLQQRSLQ----TPIVVHCSSGVGRTGAFCllyaaVQEIEAGN---- 174

                       170       180       190
                ....*....|....*....|....*....|....
gi 57659396 250 GTLSLPSVLKKVRQQKygfMNCLDD---YVLCYQ 280
Cdd:cd14539 175 GIPDLPQLVRKMRQQR---KYMLQEkehLKFCYE 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 32-287 9.47e-13

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: 66.94  E-value: 9.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  32 YALVPKHKEEGNSASAQNENKCKKELGMHLTRYLNRRIKL----RNDGRVLDASF----VDGYDFErkYICIKRLQEDAC 103
Cdd:cd14599  18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvptkENNTGYINASHikvtVGGEEWH--YIATQGPLPHTC 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 104 DKFWQAVSNYKVQIIVLISRLSD---KKCYQYW--------SSKEGCVKVSDKFRIKT-------LKIiikPHfnltLLS 165
Cdd:cd14599  96 HDFWQMVWEQGVNVIAMVTAEEEggrSKSHRYWpklgskhsSATYGKFKVTTKFRTDSgcyattgLKV---KH----LLS 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 166 ltdkfGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQTADKKIA--PIIVQCLDGISSSAVFCVFDICA 243
Cdd:cd14599 169 -----GQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCnpPIVVHCSAGVGRTGVVILTELMI 243

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 57659396 244 TQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:cd14599 244 GCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 51-240 1.29e-12

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: 66.07  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  51 NKCKkelgmhlTRYLN------RRIKL--RNDGRVLD---ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIV 119
Cdd:cd14614  12 NRCK-------NRYTNilpydfSRVKLvsMHEEEGSDyinANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 120 LISRLSDK---KCYQYWSSKEGCVKVSDkfrIKTLKIIIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWP--GDNFSHKP 193
Cdd:cd14614  85 MLTQCNEKrrvKCDHYWPFTEEPVAYGD---ITVEMLSEEEQPDWAIREFRVSYADEvQDVMHFNYTAWPdhGVPTANAA 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 57659396 194 DAFIDFycnvkdmcLQLERQTADKKIAPIIVQCLDGISSSAVFCVFD 240
Cdd:cd14614 162 ESILQF--------VQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALD 200
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 78-282 3.53e-12

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: 65.44  E-value: 3.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKE----GCVKVS--DKFRI 148
Cdd:cd14626  72 INANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKsrvKCDQYWPIRGtetyGMIQVTllDTVEL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 149 KTLKIiikphfnLTLLSLTDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdMCLQLErqtadkkIAPIIVQCLD 228
Cdd:cd14626 152 ATYSV-------RTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK-ACNPPD-------AGPMVVHCSA 216

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 57659396 229 GISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd14626 217 GVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 67-280 6.48e-12

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: 64.14  E-value: 6.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  67 RRIKLRNDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWS-SKEGCVkv 142
Cdd:cd14619  17 KPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAgrvKCEHYWPlDYTPCT-- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 143 SDKFRIKTLKIIIKPHFNLTLLSLTDKFGQEQK-ISHYQYTAWPGDNFSHKPDAFIDFYcnvkdmclQLERQTADKKIA- 220
Cdd:cd14619  95 YGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLsVRHFHFTAWPDHGVPSSTDTLLAFR--------RLLRQWLDQTMSg 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57659396 221 -PIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14619 167 gPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 26-275 1.96e-11

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: 63.13  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  26 RIIKEYYALVPKHKEEGNSASAQNENKCKKELGMHLTRYLNRRIKLRND-----GRVLDASFVDGYDFER-KYICIKRLQ 99
Cdd:cd14609  16 RLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAEsnpsrSDYINASPIIEHDPRMpAYIATQGPL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 100 EDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSkEGcvkvSDKFRIKTLKIIIK----PHFNLTLLSLTDKFGQ 172
Cdd:cd14609  96 SHTIADFWQMVWENGCTVIVMLTPLVEdgvKQCDRYWPD-EG----SSLYHIYEVNLVSEhiwcEDFLVRSFYLKNVQTQ 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 173 EQK-ISHYQYTAWPGDNFSHKPDAFIDFYCNVkDMCLQlerqtadKKIAPIIVQCLDGISSSAVFCVFDICATQFDK-TG 250
Cdd:cd14609 171 ETRtLTQFHFLSWPAEGIPSSTRPLLDFRRKV-NKCYR-------GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgVK 242

                       250       260
                ....*....|....*....|....*
gi 57659396 251 TLSLPSVLKKVRQQKYGFMNCLDDY 275
Cdd:cd14609 243 EIDIAATLEHVRDQRPGMVRTKDQF 267
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 78-279 2.39e-11

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 61.71  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFER--KYICIK-RLQEDACDkFWQAVSNYKVQIIVLISRLSDK----KCYQYWSSKEGCVKVSDKFRIKT 150
Cdd:cd17658   2 INASLVETPASESlpKFIATQgPLPHTFED-FWEMVIQQRCPVIIMLTRLVDNystaKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 151 LKIIIKPH-FNLTLLSLTDKFGQEQKIS--HYQYTAWPGDNFSHKPDAfidfycnVKDMCLQLerQTADKKIAPIIVQCL 227
Cdd:cd17658  81 KKLKHSQHsITLRVLEVQYIESEEPPLSvlHIQYPEWPDHGVPKDTRS-------VRELLKRL--YGIPPSAGPIVVHCS 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 228 DGISSSAVFCVFDICATQFDKtGTLS---LPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd17658 152 AGIGRTGAYCTIHNTIRRILE-GDMSavdLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 80-280 2.42e-11

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: 61.88  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  80 ASFVD-GYDFERKYICIKR-LQEDACDkFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSD-KFRIKTLKI 153
Cdd:cd18533   4 ASYITlPGTSSKRYIATQGpLPATIGD-FWKMIWQNNVGVIVMLTPLVENgreKCDQYWPSGEYEGEYGDlTVELVSEEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 154 IIKPHFNLTLLSLTDKFGQEQKISHYQYTAWPgdNFSHkPDAFIDFY--CNVKDMCLQLERQTadkkiAPIIVQCLDGIS 231
Cdd:cd18533  83 NDDGGFIVREFELSKEDGKVKKVYHIQYKSWP--DFGV-PDSPEDLLtlIKLKRELNDSASLD-----PPIIVHCSAGVG 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396 232 SSAVFCVFDICATQFDKTGTLSLP---------SVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd18533 155 RTGTFIALDSLLDELKRGLSDSQDledsedpvyEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 90-287 3.03e-11

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: 62.59  E-value: 3.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  90 RKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSdKFRIKTLKIIIKPHFNLTLLSL 166
Cdd:cd14606  67 KTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKgrnKCVPYWPEVGMQRAYG-PYSVTNCGEHDTTEYKLRTLQV 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 167 T--DKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlERQTADKKIAPIIVQCLDGISSSAVFCVFDICAT 244
Cdd:cd14606 146 SplDNGELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQIN------QRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLME 219

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57659396 245 QFDKTGT---LSLPSVLKKVRQQKYGFMNCLDDYVLCYQLLAVYVK 287
Cdd:cd14606 220 NISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIE 265
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 64-240 5.47e-11

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: 61.08  E-value: 5.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  64 YLNRRIKLRNDGRV-----LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSS 135
Cdd:cd14616   9 YNNNRVKLIADAGVpgsdyINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKgriRCHQYWPE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 136 KEGCVKV-------------SDKFRIKTLKIiikphfnltllsltDKFGQEQKISHYQYTAWPGDNFSHKPDAFIDFycn 202
Cdd:cd14616  89 DNKPVTVfgdivitklmedvQIDWTIRDLKI--------------ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHF--- 151

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 57659396 203 vkdmcLQLERQTADKKIAPIIVQCLDGISSSAVFCVFD 240
Cdd:cd14616 152 -----VKLVRASRAHDNTPMIVHCSAGVGRTGVFIALD 184
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 78-279 1.29e-10

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: 60.03  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKegcVKVSDKFRIKTLKII 154
Cdd:cd14631  16 INANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVgrvKCYKYWPDD---TEVYGDFKVTCVEME 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGISSS 233
Cdd:cd14631  93 PLAEYVVRTFTLERRgYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--------LSNPPSAGPIVVHCSAGAGRT 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14631 165 GCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 210
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 64-280 1.41e-10

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: 60.22  E-value: 1.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  64 YLNRRIKLRNDGRVLD----ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISR---LSDKKCYQYWSSK 136
Cdd:cd14615   9 YDISRVKLSVQSHSTDdyinANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcveQGRTKCEEYWPSK 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 137 EGcvKVSDKFRIKTLKIIIKPHFNLTLLSLTD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKDMCLQLERQta 215
Cdd:cd14615  89 QK--KDYGDITVTMTSEIVLPEWTIRDFTVKNaQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQNPPN-- 164

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 216 dkkiAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14615 165 ----SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 225
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 41-279 1.84e-10

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: 60.44  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  41 EGNSA----SAQNENKCKKELGmHLTRYLNRRIKLR-----NDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVS 111
Cdd:cd14633  26 EGQSApwdsAKKDENRMKNRYG-NIIAYDHSRVRLQpiegeTSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVW 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 112 NYKVQIIVLISRLSD---KKCYQYWSSKegcVKVSDKFRIKTLKIIIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGD 187
Cdd:cd14633 105 HENTASIIMVTNLVEvgrVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEiREIRQFHFTGWPDH 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 188 NFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYG 267
Cdd:cd14633 182 GVPYHATGLLGFVRQVK--------SKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVN 253

                       250
                ....*....|..
gi 57659396 268 FMNCLDDYVLCY 279
Cdd:cd14633 254 MVQTEEQYVFIH 265
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 26-275 5.99e-10

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: 58.91  E-value: 5.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  26 RIIKEYYALVPKHKEEGNSASAQNENKCKKELGMHLTRYLNRRIKLRNDGR-----VLDASFVDGYDFER-KYICIKRLQ 99
Cdd:cd14610  18 RLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENShshsdYINASPIMDHDPRNpAYIATQGPL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 100 EDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSkEGcvkvSDKFRIKTLKIIIK----PHFNLTLLSLTD-KFG 171
Cdd:cd14610  98 PATVADFWQMVWESGCVVIVMLTPLAEngvKQCYHYWPD-EG----SNLYHIYEVNLVSEhiwcEDFLVRSFYLKNlQTN 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 172 QEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkDMCLQlerqtadKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGT 251
Cdd:cd14610 173 ETRTVTQFHFLSWNDQGVPASTRSLLDFRRKV-NKCYR-------GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAK 244

                       250       260
                ....*....|....*....|....*
gi 57659396 252 -LSLPSVLKKVRQQKYGFMNCLDDY 275
Cdd:cd14610 245 eIDIAATLEHLRDQRPGMVQTKEQF 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 90-285 1.71e-09

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: 56.49  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  90 RKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDK---KCYQYWSSKEGCVKVSdKFRIKTLKIIIKPHFNLTLLSL 166
Cdd:cd14601  19 NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERgrvKCHQYWPEPSGSSSYG-GFQVTCHSEEGNPAYVFREMTL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 167 TD-KFGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVkdmclqleRQTADKKIAPIIVQCLDGISSSAVFCVFDICATQ 245
Cdd:cd14601  98 TNlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLV--------RNKRAGKDEPVVVHCSAGIGRTGVLITMETAMCL 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 57659396 246 FDKTGTLSLPSVLKKVRQQKYGFMNCLDDY-VLCYQLLAVY 285
Cdd:cd14601 170 IECNQPVYPLDIVRTMRDQRAMMIQTPSQYrFVCEAILKVY 210
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 49-279 2.06e-09

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: 56.96  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  49 NENKCKKELGmHLTRYLNRRIKLRN-----DGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISR 123
Cdd:cd14630   1 DENRNKNRYG-NIISYDHSRVRLQLldgdpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 124 LSD---KKCYQYWSSKE---GCVKVS-------DKFRIKTLKIIIKPHFNLtllsltdkfgqeQKISHYQYTAWPGDNFS 190
Cdd:cd14630  80 LVEvgrVKCVRYWPDDTevyGDIKVTlieteplAEYVIRTFTVQKKGYHEI------------REIRQFHFTSWPDHGVP 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 191 HKPDAFIDFYCNVKDMclqlerqtADKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMN 270
Cdd:cd14630 148 CYATGLLGFVRQVKFL--------NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQ 219


                ....*....
gi 57659396 271 CLDDYVLCY 279
Cdd:cd14630 220 TEEQYVFVH 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 44-290 2.93e-09

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: 56.86  E-value: 2.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  44 SASAQNENKCKKELGMHLTRYLNRRIKL-----RNDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQII 118
Cdd:cd14604  49 TATGEKEENVKKNRYKDILPFDHSRVKLtlktsSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAII 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 119 VLISR---LSDKKCYQYWSS-KEGCVKVSdKFRIKTLKiiIKPHFNLTLLSLTDKFGQE-QKISHYQYTAWPGDNFSHKP 193
Cdd:cd14604 129 VMACRefeMGRKKCERYWPLyGEEPMTFG-PFRISCEA--EQARTDYFIRTLLLEFQNEtRRLYQFHYVNWPDHDVPSSF 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 194 DAFIDFycnvkdmcLQLERQTADKKIAPIIVQCLDGISSSAVFCVFDICATQFdKTGTL----SLPSVLKKVRQQKYGFM 269
Cdd:cd14604 206 DSILDM--------ISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAV 276

                       250       260
                ....*....|....*....|.
gi 57659396 270 NCLDDYVLCYQLLAVYVKEKL 290
Cdd:cd14604 277 QTKEQYELVHRAIAQLFEKQL 297
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 78-279 5.05e-09

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: 55.06  E-value: 5.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKegcvkvSDKF---RIKTL 151
Cdd:cd14632   2 INANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrVKCSKYWPDD------SDTYgdiKITLL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 152 KIIIKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGI 230
Cdd:cd14632  76 KTETLAEYSVRTFALERRgYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVK--------ASTPPDAGPVVVHCSAGA 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 57659396 231 SSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14632 148 GRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIH 196
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 78-277 9.53e-09

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: 54.54  E-value: 9.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKegcVKVSDKFRIKTLKII 154
Cdd:cd14555   2 INANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvgrVKCSRYWPDD---TEVYGDIKVTLVETE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 155 IKPHFNLTLLSLTDK-FGQEQKISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGISSS 233
Cdd:cd14555  79 PLAEYVVRTFALERRgYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--------ASNPPSAGPIVVHCSAGAGRT 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 57659396 234 AVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVL 277
Cdd:cd14555 151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIF 194
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 60-282 1.64e-08

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: 54.18  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  60 HLTRYLNRRIKLRNDGR-----VLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKK---CYQ 131
Cdd:cd14618   5 HVLPYDHSRVRLSQLGGephsdYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGrvlCDH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 132 YWSSKE-----GCVKV-------SDKFRIKTLKIiikPHFNLTllsltdkfgQEQKISHYQYTAWPGDNFSHKPDAFIDF 199
Cdd:cd14618  85 YWPSEStpvsyGHITVhllaqssEDEWTRREFKL---WHEDLR---------KERRVKHLHYTAWPDHGIPESTSSLMAF 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 200 YCNVKdmclqlERQTADKKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14618 153 RELVR------EHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLH 226


                ...
gi 57659396 280 QLL 282
Cdd:cd14618 227 SCI 229
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 73-279 4.22e-08

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: 52.92  E-value: 4.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  73 NDGRVLDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISR---LSDKKCYQYWSSKEGCVKVSDKFRIK 149
Cdd:cd14602  24 EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMefeMGKKKCERYWAEPGEMQLEFGPFSVT 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 150 TLKIIIKPHFnlTLLSLTDKFGQEQKISH-YQYTAWPGDNFSHKPDAFIDFYCNVKdmCLQlerqtADKKIaPIIVQCLD 228
Cdd:cd14602 104 CEAEKRKSDY--IIRTLKVKFNSETRTIYqFHYKNWPDHDVPSSIDPILELIWDVR--CYQ-----EDDSV-PICIHCSA 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 229 GISSSAVFCVFDIcATQFDKTGTL----SLPSVLKKVRQQKYGFMNCLDDYVLCY 279
Cdd:cd14602 174 GCGRTGVICAIDY-TWMLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 78-281 1.85e-07

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: 50.79  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLS-DKKCYQYW----------------SSKEGCV 140
Cdd:cd14636   2 INAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQGCPQYWpeegmlrygpiqvecmSCSMDCD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 141 KVSDKFRIKTLKiiiKPHFNLTLlsltdkfgqeqkISHYQYTAWPgdnfSHK--PDAFIDFYcnvkDMCLQLER--QTAD 216
Cdd:cd14636  82 VISRIFRICNLT---RPQEGYLM------------VQQFQYLGWA----SHRevPGSKRSFL----KLILQVEKwqEECD 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57659396 217 KKIAPIIVQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQL 281
Cdd:cd14636 139 EGEGRTIIHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 106-283 2.40e-07

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: 50.14  E-value: 2.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 106 FWQAVSNYKVQIIVLISRLSD---KKCYQYWSSKEGcvKVSDKFRIKtlkiIIKPHF--------NLTLLSLtdKFGQEQ 174
Cdd:cd14546  31 FWQMIWEQGCVVIVMLTRLQEngvKQCARYWPEEGS--EVYHIYEVH----LVSEHIwcddylvrSFYLKNL--QTSETR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 175 KISHYQYTAWPGDNFSHKPDAFIDFYCNVKdmclqlerQTADKKIAPIIVQCLDGISSSAVFCVFDICATQFDK-TGTLS 253
Cdd:cd14546 103 TVTQFHFLSWPDEGIPASAKPLLEFRRKVN--------KSYRGRSCPIVVHCSDGAGRTGTYILIDMVLNRMAKgAKEID 174

                       170       180       190
                ....*....|....*....|....*....|
gi 57659396 254 LPSVLKKVRQQKYGFMNCLDDYVLCYQLLA 283
Cdd:cd14546 175 IAATLEHLRDQRPGMVKTKDQFEFVLTAVA 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 78-282 5.04e-07

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: 49.22  E-value: 5.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLIS---RLSDKKCYqYWSSKEGCVkVSDKFRIKTL--- 151
Cdd:cd17669   2 INASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPdgqNMAEDEFV-YWPNKDEPI-NCETFKVTLIaee 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 152 --------KIIIKphfNLTLLSLTDKFGQEqkISHYQYTAWPgdnfshKPDAFIDFYCNVkdmcLQLERQTADKKIAPII 223
Cdd:cd17669  80 hkclsneeKLIIQ---DFILEATQDDYVLE--VRHFQCPKWP------NPDSPISKTFEL----ISIIKEEAANRDGPMI 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57659396 224 VQCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd17669 145 VHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 78-282 2.90e-06

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: 46.98  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLI---SRLSDKKcYQYWSSKE---GC----VKVSDKFR 147
Cdd:cd17670   2 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDE-FVYWPSREesmNCeaftVTLISKDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 148 I---KTLKIIIKphfNLTLLSLTDKFGQEqkISHYQYTAWPgdnfshKPDAFIDFYCNVkdmcLQLERQTADKKIAPIIV 224
Cdd:cd17670  81 LclsNEEQIIIH---DFILEATQDDYVLE--VRHFQCPKWP------NPDAPISSTFEL----INVIKEEALTRDGPTIV 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57659396 225 QCLDGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQLL 282
Cdd:cd17670 146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 78-281 2.99e-06

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: 46.99  E-value: 2.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKK-CYQYWSskEGCVKVSDKFRIKTLKIIIK 156
Cdd:cd14635   2 INAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQlCPQYWP--ENGVHRHGPIQVEFVSADLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 157 PHFNLTLLSLTDKFGQE---QKISHYQYTAWPgdNFSHKPDAFIDFycnvkdmcLQLERQTA------DKKIAPIIVQCL 227
Cdd:cd14635  80 EDIISRIFRIYNAARPQdgyRMVQQFQFLGWP--MYRDTPVSKRSF--------LKLIRQVDkwqeeyNGGEGRTVVHCL 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 57659396 228 DGISSSAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQL 281
Cdd:cd14635 150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 80-280 1.19e-05

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: 45.00  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  80 ASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRL-SDKKCYQYWSSKEGCVKvSDKFRIKTLKIIIKPH 158
Cdd:cd14550   4 ASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNeLNEDEPIYWPTKEKPLE-CETFKVTLSGEDHSCL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 159 FNLTLLSLTD------KFGQEQKISHYQYTAWPgdNFSHKPDAFIDFYCNVKDMCLQLErqtadkkiAPIIVQCLDGISS 232
Cdd:cd14550  83 SNEIRLIVRDfilestQDDYVLEVRQFQCPSWP--NPCSPIHTVFELINTVQEWAQQRD--------GPIVVHDRYGGVQ 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 57659396 233 SAVFCVFDICATQFDKTGTLSLPSVLKKVRQQKYGFMNCLDDYVLCYQ 280
Cdd:cd14550 153 AATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 78-281 3.36e-05

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: 44.13  E-value: 3.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396  78 LDASFVDGYDFERKYICIKRLQEDACDKFWQAVSNYKVQIIVLISRLSDKK----CYQYWSSK-------------EGCV 140
Cdd:cd14637   2 INAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNsawpCLQYWPEPglqqygpmevefvSGSA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 141 K---VSDKFRIKTLKIIIKPHFnltllsltdkfgqeqKISHYQYTAWPGdnFSHKPD---AFIDFYCNVKdmclQLERQT 214
Cdd:cd14637  82 DediVTRLFRVQNITRLQEGHL---------------MVRHFQFLRWSA--YRDTPDskkAFLHLLASVE----KWQRES 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57659396 215 ADKKIapiIVQCLDGISSSAVFCVfdiCATQFDKTGTLSLPSVL---KKVRQQKYGFMNCLDDYVLCYQL 281
Cdd:cd14637 141 GEGRT---VVHCLNGGGRSGTYCA---SAMILEMIRCHNIVDVFyavKTLRNYKPNMVETLEQYRFCYEI 204
 
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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