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Conserved domains on  [gi|313199514|emb|CAS06625|]
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protein tyrosine phosphatase, partial [Bracoviriform melanoscelae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02740 super family cl31499
protein tyrosine phosphatase; Provisional
 1-248 5.85e-54

protein tyrosine phosphatase; Provisional


The actual alignment was detected with superfamily member PHA02740:

Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 175.93  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   1 LLFMDNVDSFDLIRLEYYII-----EQNRKICEVSD----DEPDNKWCRQLLHRF--LCCMKRYLRADFIDGYDaydRQR 69
Cdd:PHA02740  15 INFINKPDLLSCIIKEYRAIvpeheDEANKACAQAEnkakDENLALHITRLLHRRikLFNDEKVLDARFVDGYD---FEQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  70 KYICISDPKAENYEKFWELAWCREVNTIVKISQREEESC--QYWSSREGSEIECGGFRIKTLIVIKRPRFISTLLLLSDQ 147
Cdd:PHA02740  92 KFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCfnQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 148 KNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKeQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKY 227
Cdd:PHA02740 172 FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEK-HKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                        250       260
                 ....*....|....*....|.
gi 313199514 228 TGTISVANAYRKIKQREHNCL 248
Cdd:PHA02740 251 TGMLSIANALKKVRQKKYGCM 271
 
Name Accession Description Interval E-value
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-248 5.85e-54

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 175.93  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   1 LLFMDNVDSFDLIRLEYYII-----EQNRKICEVSD----DEPDNKWCRQLLHRF--LCCMKRYLRADFIDGYDaydRQR 69
Cdd:PHA02740  15 INFINKPDLLSCIIKEYRAIvpeheDEANKACAQAEnkakDENLALHITRLLHRRikLFNDEKVLDARFVDGYD---FEQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  70 KYICISDPKAENYEKFWELAWCREVNTIVKISQREEESC--QYWSSREGSEIECGGFRIKTLIVIKRPRFISTLLLLSDQ 147
Cdd:PHA02740  92 KFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCfnQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 148 KNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKeQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKY 227
Cdd:PHA02740 172 FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEK-HKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                        250       260
                 ....*....|....*....|.
gi 313199514 228 TGTISVANAYRKIKQREHNCL 248
Cdd:PHA02740 251 TGMLSIANALKKVRQKKYGCM 271
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
53-243 9.25e-27

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 103.89  E-value: 9.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514    53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECGGFRIKT 128
Cdd:smart00194  56 YINASYIDGPN---GPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEkgrEKCaQYWPDEEGEPLTYGDITVTL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   129 LIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHCND 207
Cdd:smart00194 133 KSVEKVDDYTIRTLEVTNTGCSEtRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST---------GPIVVHCSA 203

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 313199514   208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:smart00194 204 GVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELrSQR 240
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 53-243 2.58e-26

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: 101.21  E-value: 2.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSREGSEIECGGFRIKT 128
Cdd:cd00047    1 YINASYIDGYR---GPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgreKCERYWPEEGGKPLEYGDITVTL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHCND 207
Cdd:cd00047   78 VSEEELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN---------GPIVVHCSA 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:cd00047  149 GVGRTGTFIAIDILLERLEAEGEVDVFEIVKALrKQR 185
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
53-243 1.77e-23

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 94.62  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECGGFRIKT 128
Cdd:pfam00102  29 YINASYIDGYK---KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEkgrEKCaQYWPEEEGESLEYGDFTVTL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  129 L-IVIKRPRFISTLLLLS-DQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLndtyttskKEQSAEWKLGTVLVHCN 206
Cdd:pfam00102 106 KkEKEDEKDYTVRTLEVSnGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV--------RKSSLDGRSGPIVVHCS 177

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 313199514  207 DGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:pfam00102 178 AGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELrSQR 215
 
Name Accession Description Interval E-value
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1-248 5.85e-54

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 175.93  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   1 LLFMDNVDSFDLIRLEYYII-----EQNRKICEVSD----DEPDNKWCRQLLHRF--LCCMKRYLRADFIDGYDaydRQR 69
Cdd:PHA02740  15 INFINKPDLLSCIIKEYRAIvpeheDEANKACAQAEnkakDENLALHITRLLHRRikLFNDEKVLDARFVDGYD---FEQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  70 KYICISDPKAENYEKFWELAWCREVNTIVKISQREEESC--QYWSSREGSEIECGGFRIKTLIVIKRPRFISTLLLLSDQ 147
Cdd:PHA02740  92 KFICIINLCEDACDKFLQALSDNKVQIIVLISRHADKKCfnQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDK 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 148 KNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKeQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKY 227
Cdd:PHA02740 172 FGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEK-HKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                        250       260
                 ....*....|....*....|.
gi 313199514 228 TGTISVANAYRKIKQREHNCL 248
Cdd:PHA02740 251 TGMLSIANALKKVRQKKYGCM 271
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 10-245 7.29e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 110.86  E-value: 7.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  10 FDLIRLEYY--IIEQNRKICEVS---DDEPDNKWC--------RQLLHRFLCCMKRYLRADFIDGYDaydRQRKYICISD 76
Cdd:PHA02747  24 FGIIRDEHHqiILKPFDGLIANFekpENQPKNRYWdipcwdhnRVILDSGGGSTSDYIHANWIDGFE---DDKKFIATQG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  77 PKAENYEKFWELAWCREVNTIV-----KISQREEESCQYWSSREGSEIECGGFRIKTLIVIKRPRFISTLLLLSDQ-KNR 150
Cdd:PHA02747 101 PFAETCADFWKAVWQEHCSIIVmltptKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKiLKD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 151 KREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEQSAEWK-LGTVLVHCNDGSSFSAVYCVLDMCVTQFKYTG 229
Cdd:PHA02747 181 SRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPKDAlLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRK 260

                        250
                 ....*....|....*.
gi 313199514 230 TISVANAYRKIKQREH 245
Cdd:PHA02747 261 AICLAKTAEKIREQRH 276
PHA02738 PHA02738
hypothetical protein; Provisional
 53-248 2.70e-28

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 109.63  E-value: 2.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECGGFRIKT 128
Cdd:PHA02738  77 YINANYVDGFE---YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEngrEKCfPYWSDVEQGSIRFGKFKITT 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSL----NDTYTTSKKEQSAEWKLGTVLVH 204
Cdd:PHA02738 154 TQVETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVrqcqKELAQESLQIGHNRLQPPPIVVH 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313199514 205 CNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHNCL 248
Cdd:PHA02738 234 CNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSL 277
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 53-246 7.08e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 108.58  E-value: 7.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAYDrqrKYICISDPKAENYEKFWELAWCREVNTIVKISQ--REEESC-QYWSSREGSEIECGGFRIKTL 129
Cdd:PHA02746 100 YIHANFVDGFKEAN---KFICAQGPKEDTSEDFFKLISEHESQVIVSLTDidDDDEKCfELWTKEEDSELAFGRFVAKIL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 130 IVIKRPRFISTLLLLSDQ-KNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKE-QSAEWKLGTVLVHCND 207
Cdd:PHA02746 177 DIIEELSFTKTRLMITDKiSDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQaDNDPQTLGPIVVHCSA 256

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:PHA02746 257 GIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHS 295
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
53-243 9.25e-27

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 103.89  E-value: 9.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514    53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECGGFRIKT 128
Cdd:smart00194  56 YINASYIDGPN---GPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEkgrEKCaQYWPDEEGEPLTYGDITVTL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   129 LIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHCND 207
Cdd:smart00194 133 KSVEKVDDYTIRTLEVTNTGCSEtRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTST---------GPIVVHCSA 203

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 313199514   208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:smart00194 204 GVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELrSQR 240
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 53-243 2.58e-26

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: 101.21  E-value: 2.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSREGSEIECGGFRIKT 128
Cdd:cd00047    1 YINASYIDGYR---GPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgreKCERYWPEEGGKPLEYGDITVTL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHCND 207
Cdd:cd00047   78 VSEEELSDYTIRTLELSPKGCSEsREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN---------GPIVVHCSA 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:cd00047  149 GVGRTGTFIAIDILLERLEAEGEVDVFEIVKALrKQR 185
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 53-248 2.01e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 98.92  E-value: 2.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSREGSEIECGGFRIKT 128
Cdd:PHA02742  80 FINASYVDGHNA---KGRFICTQAPLEETALDFWQAIFQDQVRVIVmitKIMEDGKEACyPYWMPHERGKATHGEFKIKT 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LiVIKRPRF--ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEQSAE--WKLGTVLVH 204
Cdd:PHA02742 157 K-KIKSFRNyaVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGEniVKEPPILVH 235

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313199514 205 CNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHNCL 248
Cdd:PHA02742 236 CSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCL 279
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
53-243 1.77e-23

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 94.62  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECGGFRIKT 128
Cdd:pfam00102  29 YINASYIDGYK---KPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEkgrEKCaQYWPEEEGESLEYGDFTVTL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  129 L-IVIKRPRFISTLLLLS-DQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLndtyttskKEQSAEWKLGTVLVHCN 206
Cdd:pfam00102 106 KkEKEDEKDYTVRTLEVSnGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV--------RKSSLDGRSGPIVVHCS 177

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 313199514  207 DGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI-KQR 243
Cdd:pfam00102 178 AGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELrSQR 215
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 53-245 8.45e-21

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: 87.02  E-value: 8.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SC-QYWSSrEGSEiECGGFRIKT 128
Cdd:cd14549    1 YINANYVDGYN---KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgrrKCdQYWPK-EGTE-TYGNIQVTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRK-------REILHYHYTASPTNNNSDEPFIFLSFVcslndtyttsKKEQSAE-WKLGT 200
Cdd:cd14549   76 LSTEVLATYTVRTFSLKNLKLKKvkgrsseRVVYQYHYTQWPDHGVPDYTLPVLSFV----------RKSSAANpPGAGP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 313199514 201 VLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd14549  146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRtQRNY 191
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 53-245 4.54e-20

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: 85.03  E-value: 4.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SC-QYWSSrEGSEiECGGF---- 124
Cdd:cd17668    1 YINANYVDGYN---KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKgrrKCdQYWPA-DGSE-EYGNFlvtq 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 125 -RIKTLIVIKRPRFI--STLLLLSDQKNRK--REILHYHYTASPTNNNSDEPFIFLSFVcslndtyttSKKEQSAEWKLG 199
Cdd:cd17668   76 kSVQVLAYYTVRNFTlrNTKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYTLPVLTFV---------RKASYAKRHAVG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 313199514 200 TVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd17668  147 PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRsQRNY 193
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 53-245 1.02e-19

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: 85.49  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYdaydRQRK-YICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SC-QYWSSREGSEIECGGFRIK 127
Cdd:cd14543   59 YINANFMDGY----KQKNaYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERgrvKCgQYWPLEEGSSLRYGDLTVT 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASP---TNNNSDEPFIFLSFVcslNDTYTTSKKEQSAEWK----LG 199
Cdd:cd14543  135 NLSVENKEHYkKTTLEIHNTETDESRQVTHFQFTSWPdfgVPSSAAALLDFLGEV---RQQQALAVKAMGDRWKghppGP 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 313199514 200 TVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd14543  212 PIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRtQRAF 258
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 53-233 7.88e-19

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: 82.44  E-value: 7.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES---C-QYWSSReGSEIeCGGFRIKT 128
Cdd:cd14553   33 YINANYCDGYR---KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEERSrvkCdQYWPTR-GTET-YGLIQVTL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFV-----CSLNDTyttskkeqsaewklGTVL 202
Cdd:cd14553  108 LDTVELATYtVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLrrvkaCNPPDA--------------GPIV 173

                        170       180       190
                 ....*....|....*....|....*....|.
gi 313199514 203 VHCNDGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14553  174 VHCSAGVGRTGCFIVIDSMLERIKHEKTVDI 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 53-222 8.17e-17

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: 77.76  E-value: 8.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES----CQYWSSREGSEI--ECGGFRI 126
Cdd:cd14608   51 YINASLIKMEEA---QRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGslkcAQYWPQKEEKEMifEDTNLKL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 127 kTLIV--IKRPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewKLGTVLVH 204
Cdd:cd14608  128 -TLISedIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSP-------EHGPVVVH 199

                        170
                 ....*....|....*...
gi 313199514 205 CNDGSSFSAVYCVLDMCV 222
Cdd:cd14608  200 CSAGIGRSGTFCLADTCL 217
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 53-233 1.93e-16

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: 76.61  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES---C-QYWSSReGSEIeCGGFRIKT 128
Cdd:cd14626   71 YINANYIDGYR---KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSrvkCdQYWPIR-GTET-YGMIQVTL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFV-----CSLNDTyttskkeqsaewklGTVL 202
Cdd:cd14626  146 LDTVELATYsVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLrrvkaCNPPDA--------------GPMV 211

                        170       180       190
                 ....*....|....*....|....*....|.
gi 313199514 203 VHCNDGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14626  212 VHCSAGVGRTGCFIVIDAMLERMKHEKTVDI 242
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 53-243 6.72e-15

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: 72.45  E-value: 6.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECggFRIKT 128
Cdd:cd14629   83 YINASFIDGYR---QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmgrEKChQYWPAERSARYQY--FVVDP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKN-RKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTyttskKEQSAEwkLGTVLVHCND 207
Cdd:cd14629  158 MAEYNMPQYILREFKVTDARDgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKT-----KEQFGQ--DGPITVHCSA 230

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14629  231 GVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQ 266
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 53-243 1.07e-14

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: 71.69  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECggFRIKT 128
Cdd:cd14627   83 YINASFIDGYR---QQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREmgrEKChQYWPAERSARYQY--FVVDP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKN-RKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTyttskKEQSAEwkLGTVLVHCND 207
Cdd:cd14627  158 MAEYNMPQYILREFKVTDARDgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKT-----KEQFGQ--DGPISVHCSA 230

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14627  231 GVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 266
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 53-243 1.17e-14

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: 71.69  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREGSEIECggFRIKT 128
Cdd:cd14628   82 YINASFIDGYR---QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREmgrEKChQYWPAERSARYQY--FVVDP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKN-RKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTyttskKEQSAEwkLGTVLVHCND 207
Cdd:cd14628  157 MAEYNMPQYILREFKVTDARDgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKT-----KEQFGQ--DGPISVHCSA 229

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14628  230 GVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQ 265
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 52-233 2.37e-14

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: 70.11  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  52 RYLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSREGSEIEC--GGFR 125
Cdd:cd14545   25 DYINASLVEVEEA---KRSYILTQGPLPNTSGHFWQMVWEQNSKAVImlnKLMEKGQIKCaQYWPQGEGNAMIFedTGLK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 126 IKTLIVIKRPRFISTLLLLSDQK-NRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTyttskkeQSAEWKLGTVLVH 204
Cdd:cd14545  102 VTLLSEEDKSYYTVRTLELENLKtQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRES-------GSLSSDVGPPVVH 174

                        170       180
                 ....*....|....*....|....*....
gi 313199514 205 CNDGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14545  175 CSAGIGRSGTFCLVDTCLVLIEKGNPSSV 203
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 53-233 2.94e-14

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: 69.73  E-value: 2.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDayDRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE--ESC-QYWSSREGSEIecGGFRIKTL 129
Cdd:cd14547   27 YINANYIRGYD--GEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEakEKCaQYWPEEENETY--GDFEVTVQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 130 IVIKRPRFISTLLLLSdQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTyttskkeQSAEWKLGTVLVHCNDGS 209
Cdd:cd14547  103 SVKETDGYTVRKLTLK-YGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA-------RQTEPHRGPIVVHCSAGI 174

                        170       180
                 ....*....|....*....|....
gi 313199514 210 SFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14547  175 GRTGCFIATSIGCQQLREEGVVDV 198
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 53-233 3.86e-14

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: 69.48  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYdaydRQRK-YICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSREGSEIecGGFRIK 127
Cdd:cd14554   36 YINASFIDGY----RQRGaYIATQGPLAETTEDFWRMLWEHNSTIIVmltKLREMGREKChQYWPAERSARY--QYFVVD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEqsaewklGTVLVHCN 206
Cdd:cd14554  110 PMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQE-------GPITVHCS 182

                        170       180
                 ....*....|....*....|....*..
gi 313199514 207 DGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14554  183 AGVGRTGVFITLSIVLERMRYEGVVDV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-233 4.93e-14

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: 69.48  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  52 RYLRADFIDGYDAydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE--ESCQ-YWSSREGS----EI----- 119
Cdd:cd14612   45 SYINANYIRGYDG--KEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEkkEKCVhYWPEKEGTygrfEIrvqdm 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 120 -ECGGFRIKTLIVikrprfistllllsDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewKL 198
Cdd:cd14612  123 kECDGYTIRDLTI--------------QLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEESRQTAA-------SP 181

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 313199514 199 GTVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14612  182 GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDI 216
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 53-245 5.80e-14

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: 68.45  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAYDrqrKYICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSrEGSeIECGGFRIKt 128
Cdd:cd14552    1 YINASFIDGYRQKD---AYIATQGPLDHTVEDFWRMIWEWKSCSIVmltEIKERSQNKCaQYWPE-DGS-VSSGDITVE- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 livIKRPRF-----ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAEwklGTVLV 203
Cdd:cd14552   75 ---LKDQTDyedytLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQ-----KQQQQSGN---HPITV 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313199514 204 HCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd14552  144 HCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRlQRPH 186
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 53-245 2.48e-13

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: 66.99  E-value: 2.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSrEGSeIECGGFRIKt 128
Cdd:cd14623   26 YVNASFIDGYR---QKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgqEKCaQYWPS-DGS-VSYGDITIE- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 livIKRPR-----FISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAEwklGTVLV 203
Cdd:cd14623  100 ---LKKEEecesyTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQ-----KQQQQSGN---HPITV 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313199514 204 HCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd14623  169 HCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRlQRPH 211
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 53-248 2.62e-13

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: 66.39  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSREGSEIECGGFRIKT 128
Cdd:cd14557    1 YINASYIDGFKE---PRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEgnrnKCAQYWPSMEEGSRAFGDVVVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNR--KREILHYHYTASPTNNNSDEPFIFLSF---VCSLNDTYTtskkeqsaewklGTVLV 203
Cdd:cd14557   78 NEEKICPDYIIRKLNINNKKEKgsGREVTHIQFTSWPDHGVPEDPHLLLKLrrrVNAFNNFFS------------GPIVV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 313199514 204 HCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYrkIKQREHNCL 248
Cdd:cd14557  146 HCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYV--VKLRRQRCL 188
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 53-245 2.81e-13

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: 66.57  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYdaydRQRKY-ICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSrEGSeIECGGFRIK 127
Cdd:cd14622    2 YINASFIDGY----RQKDYfIATQGPLAHTVEDFWRMVWEWKCHTIVmltELQEREQEKCvQYWPS-EGS-VTHGEITIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 tlivIKRPRFISTL-----LLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAEwklGTVL 202
Cdd:cd14622   76 ----IKNDTLLETIsirdfLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQ-----KQQQQTGN---HPIV 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 313199514 203 VHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK-QREH 245
Cdd:cd14622  144 VHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRlQRPH 187
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 53-246 3.72e-13

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: 66.23  E-value: 3.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSsrEGSEIEcGGFRIKT 128
Cdd:cd14632    1 YINANYIDGYH---RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEvgrvKCSKYWP--DDSDTY-GDIKITL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVcslndtyttSKKEQSAEWKLGTVLVHCND 207
Cdd:cd14632   75 LKTETLAEYsVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFI---------RRVKASTPPDAGPVVVHCSA 145

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:cd14632  146 GAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRIN 184
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 53-222 1.20e-12

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: 65.76  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSREGSEIECG--GFRI 126
Cdd:cd14607   50 YINASLVVIEEA---QRSYILTQGPLPNTCCHFWLMVWQQKTKAVVmlnRIVEKDSVKCaQYWPTDEEEVLSFKetGFSV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 127 KTLIVIKRPRFISTLLLLSDQKN-RKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEqsaewklGTVLVHC 205
Cdd:cd14607  127 KLLSEDVKSYYTVHLLQLENINSgETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEH-------GPAVVHC 199

                        170
                 ....*....|....*..
gi 313199514 206 NDGSSFSAVYCVLDMCV 222
Cdd:cd14607  200 SAGIGRSGTFSLVDTCL 216
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 53-246 1.35e-11

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: 61.86  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSsrEGSEIEcGGFRIkT 128
Cdd:cd14555    1 YINANYIDGYH---RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEvgrvKCSRYWP--DDTEVY-GDIKV-T 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIK--RPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAewklGTVLVHCN 206
Cdd:cd14555   74 LVETEplAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-----ASNPPSA----GPIVVHCS 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 313199514 207 DGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVN 184
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 85-241 2.24e-11

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: 62.09  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  85 FWELAWCREVNTIV---KISQREEESC-QYWSSrEGSEIECGGFRIKTLIVIKRPRFISTLLLLS--DQKNRKREILHYH 158
Cdd:cd14544   68 FWSMVWQENSRVIVmttKEVERGKNKCvRYWPD-EGMQKQYGPYRVQNVSEHDTTDYTLRELQVSklDQGDPIREIWHYQ 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 159 YTASPTNNNSDEPFIFLSFVCSLNdtyttskKEQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYR 238
Cdd:cd14544  147 YLSWPDHGVPSDPGGVLNFLEDVN-------QRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQK 219


                 ...
gi 313199514 239 KIK 241
Cdd:cd14544  220 TIQ 222
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 53-248 3.87e-11

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: 60.48  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAYdrQRKYICISDPKAENYEKFWELAWCREVNTIVKIsQREEESCQ-----YWSSREGSEIECGGFRIK 127
Cdd:cd14539    1 YINASLIEDLTPY--CPRFIATQAPLPGTAADFWLMVYEQQVSVIVML-VSEQENEKqkvhrYWPTERGQALVYGAITVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKRPRFISTLLLLSDQKNR-KREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEQSAewklgtVLVHCN 206
Cdd:cd14539   78 LQSVRTTPTHVERIISIQHKDTRlSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTP------IVVHCS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313199514 207 DGSSFSAVYCVLDMCVTQFKY-TGTISVANAYRKIKQREHNCL 248
Cdd:cd14539  152 SGVGRTGAFCLLYAAVQEIEAgNGIPDLPQLVRKMRQQRKYML 194
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 53-246 1.13e-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: 59.65  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSsrEGSEIEcGGFRIKT 128
Cdd:cd14631   15 YINANYIDGYQ---RPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEvgrvKCYKYWP--DDTEVY-GDFKVTC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVcslndtyttSKKEQSAEWKLGTVLVHCND 207
Cdd:cd14631   89 VEMEPLAEYvVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFI---------RRVKLSNPPSAGPIVVHCSA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:cd14631  160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRIN 198
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 53-235 1.47e-10

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: 59.19  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES---CQ-YWSSrEGSEIECGGFRIKT 128
Cdd:cd14618   27 YINANFIPGYTS---PQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGrvlCDhYWPS-ESTPVSYGHITVHL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEqsaewklGTVLVHCND 207
Cdd:cd14618  103 LAQSSEDEWTRREFKLWHEDLRKeRRVKHLHYTAWPDHGIPESTSSLMAFRELVREHVQATKGK-------GPTLVHCSA 175

                        170       180
                 ....*....|....*....|....*...
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVAN 235
Cdd:cd14618  176 GVGRSGTFIALDRLLRQLKEEKVVDVFN 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 53-243 1.70e-10

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: 58.77  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKIS---QREEESC-QYWSSRegSEIECGGFRIKT 128
Cdd:cd14551    1 YINASYIDGYQ---EKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTnlkERKEKKCsQYWPDQ--GCWTYGNLRVRV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQ-----KNRKREILHYHYTASPTNNNSDEPFIFLSF---VCSLNDTYTtskkeqsaewklGT 200
Cdd:cd14551   76 EDTVVLVDYTTRKFCIQKVnrgigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFlkkVKSANPPRA------------GP 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313199514 201 VLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14551  144 IVVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQ 186
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 53-248 2.14e-10

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: 58.90  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYWSSREgSEIECGGFRIKT 128
Cdd:cd14548   26 YINANYIPGYNS---PREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEkgrVKCdHYWPFDQ-DPVYYGDITVTM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSdQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDtytTSKKEQsaewklGTVLVHCNDG 208
Cdd:cd14548  102 LSESVLPDWTIREFKLE-RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD---YIKQEK------GPTIVHCSAG 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 313199514 209 SSFSAVYCVLDMCVTQFKYTGTISVANAYRKIkqREHNCL 248
Cdd:cd14548  172 VGRTGTFIALDRLLQQIESEDYVDIFGIVYDL--RKHRPL 209
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 53-218 3.79e-10

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: 57.79  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQ----REEESCQYWSSREGS--EIEcggfrI 126
Cdd:cd14558    1 YINASFIDGYWG---PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElkegDQEQCAQYWGDEKKTygDIE-----V 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 127 KTLIVIKRPRFI-STLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDT--YTTSKKEQSAewklgTVLV 203
Cdd:cd14558   73 ELKDTEKSPTYTvRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKlpYKNSKHGRSV-----PIVV 147

                        170
                 ....*....|....*
gi 313199514 204 HCNDGSSFSAVYCVL 218
Cdd:cd14558  148 HCSDGSSRTGIFCAL 162
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 65-226 6.37e-10

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: 57.26  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  65 YDRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES----CQYWSSREGsEIECGGFRIKtLI---VIKRPRF 137
Cdd:cd18533   11 GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGrekcDQYWPSGEY-EGEYGDLTVE-LVseeENDDGGF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 138 ISTLLLLSDQKNRKREILHYHYTASPTNN--NSDEPFIFLSFVcslndtyttSKKEQSAEWKLGTVLVHCNDGSSFSAVY 215
Cdd:cd18533   89 IVREFELSKEDGKVKKVYHIQYKSWPDFGvpDSPEDLLTLIKL---------KRELNDSASLDPPIIVHCSAGVGRTGTF 159

                        170
                 ....*....|.
gi 313199514 216 CVLDMCVTQFK 226
Cdd:cd18533  160 IALDSLLDELK 170
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 53-246 8.94e-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: 57.75  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSsrEGSEIecggFRIKT 128
Cdd:cd14633   70 YINGNYIDGYH---RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvgrvKCCKYWP--DDTEI----YKDIK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF----ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAewklGTVLVH 204
Cdd:cd14633  141 VTLIETELLaeyvIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVK-----SKSPPNA----GPLVVH 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313199514 205 CNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:cd14633  212 CSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVN 253
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 53-243 9.14e-10

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: 57.26  E-value: 9.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKIS---QREEESC-QYWSSrEGSEIEcGGFRIK- 127
Cdd:cd14620   25 YINASYIDGYK---EKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTnlkERKEEKCyQYWPD-QGCWTY-GNIRVAv 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 ---TLIVIKRPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSF---VCSLNDTYTtskkeqsaewklGTV 201
Cdd:cd14620  100 edcVVLVDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFlkkVKSVNPVHA------------GPI 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313199514 202 LVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14620  168 VVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQ 209
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 53-220 1.20e-09

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: 56.30  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIdgYDAYDRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSrEGSEIEcGGFRIkT 128
Cdd:cd14546    1 YINASTI--YDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEngvkQCARYWPE-EGSEVY-HIYEV-H 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LI---VIKRPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYttskKEQSAewklgTVLVHC 205
Cdd:cd14546   76 LVsehIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY----RGRSC-----PIVVHC 146

                        170
                 ....*....|....*
gi 313199514 206 NDGSSFSAVYCVLDM 220
Cdd:cd14546  147 SDGAGRTGTYILIDM 161
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 66-214 1.94e-09

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: 55.93  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  66 DRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE---ESC-QYW--SSREGSEIECGGFRIKTLIVIKRPRFIS 139
Cdd:cd14540   13 GKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEggrEKCfRYWptLGGEHDALTFGEYKVSTKFSVSSGCYTT 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313199514 140 TLLLLSD-QKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEQSAEWKLGTVLVHCNDGSSFSAV 214
Cdd:cd14540   93 TGLRVKHtLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLVHCSAGVGRTGV 168
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 53-233 2.77e-09

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: 55.40  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQRE--EESCQYWSSrEGSEIECGGFRI---- 126
Cdd:cd14550    1 YINASYLQGYR---RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNElnEDEPIYWPT-KEKPLECETFKVtlsg 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 127 -KTLIVIKRPRFIST-LLLLSDQKNRKREILHYHYTASPTNNNSdepfifLSFVCSLNDTYTTSKKEQSaewklGTVLVH 204
Cdd:cd14550   77 eDHSCLSNEIRLIVRdFILESTQDDYVLEVRQFQCPSWPNPCSP------IHTVFELINTVQEWAQQRD-----GPIVVH 145

                        170       180
                 ....*....|....*....|....*....
gi 313199514 205 CNDGSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14550  146 DRYGGVQAATFCALTTLHQQLEHESSVDV 174
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 53-233 1.45e-08

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: 53.67  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES---C-QYWSSREGSEIecGGFRIKT 128
Cdd:cd14615   26 YINANYMPGYN---SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGrtkCeEYWPSKQKKDY--GDITVTM 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEqsaewklGTVLVHCND 207
Cdd:cd14615  101 TSEIVLPEWtIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQNPPN-------SPILVHCSA 173

                        170       180
                 ....*....|....*....|....*.
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISV 233
Cdd:cd14615  174 GVGRTGTFIAIDRLIYQIENENVVDV 199
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 53-235 2.70e-08

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: 53.00  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE--ESC-QYWSSREG----------SEI 119
Cdd:cd14611   30 YINANYIRGYGG--KEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEknEKCvLYWPEKRGiygkvevlvnSVK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 120 ECGGFRIKTLIVikrprfistllllsDQKNRKREILHYHYTASPTNNNSD--EPFIFLsfvcsLNDTYTTSKKEQSAewk 197
Cdd:cd14611  108 ECDNYTIRNLTL--------------KQGSQSRSVKHYWYTSWPDHKTPDsaQPLLQL-----MLDVEEDRLASPGR--- 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 313199514 198 lGTVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVAN 235
Cdd:cd14611  166 -GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLS 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 53-219 4.39e-08

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: 52.52  E-value: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVkISQREEE----SCQ-YWSSREGSeIECGGFRIk 127
Cdd:cd14603   60 YINANFIKGVD---GSRAYIATQGPLSHTVLDFWRMIWQYGVKVIL-MACREIEmgkkKCErYWAQEQEP-LQTGPFTI- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKRPRFISTLLLLS-DQKNRKREILHYHYTASPTNNNSDEPFIFLSFVcSLNDTYTTSKKEqsaewklgTVLVHCN 206
Cdd:cd14603  134 TLVKEKRLNEEVILRTLKvTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMI-ELARRLQGSGPE--------PLCVHCS 204

                        170
                 ....*....|...
gi 313199514 207 DGSSFSAVYCVLD 219
Cdd:cd14603  205 AGCGRTGVICTVD 217
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-246 4.96e-08

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: 52.34  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSsregSEIECGGfRIKT 128
Cdd:cd14630   33 YINANYIDGYH---RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEvgrvKCVRYWP----DDTEVYG-DIKV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRP---RFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHC 205
Cdd:cd14630  105 TLIETEPlaeYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFLNPPDA---------GPIVVHC 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 313199514 206 NDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQREHN 246
Cdd:cd14630  176 SAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVN 216
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
153-245 5.81e-08

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 49.66  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   153 EILHYHYTASPTNNNSDEPFIFLSFVcslndtyTTSKKEQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKY-TGTI 231
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELL-------RAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                           90
                   ....*....|....*
gi 313199514   232 SVANAYRKI-KQREH 245
Cdd:smart00404  74 DIFDTVKELrSQRPG 88
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 153-245 5.81e-08

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: 49.66  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514   153 EILHYHYTASPTNNNSDEPFIFLSFVcslndtyTTSKKEQSAEWKLGTVLVHCNDGSSFSAVYCVLDMCVTQFKY-TGTI 231
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELL-------RAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEV 73

                           90
                   ....*....|....*
gi 313199514   232 SVANAYRKI-KQREH 245
Cdd:smart00012  74 DIFDTVKELrSQRPG 88
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 69-224 6.22e-08

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: 51.48  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  69 RKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSREGSEiECGGFRIKTLIVIKRPRFISTLLLL 144
Cdd:cd14601   19 NRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVErgrvKCHQYWPEPSGSS-SYGGFQVTCHSEEGNPAYVFREMTL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 145 SD-QKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttSKKEQSAEwklgTVLVHCNDGSSFSAVYCVLD--MC 221
Cdd:cd14601   98 TNlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR-----NKRAGKDE----PVVVHCSAGIGRTGVLITMEtaMC 168


                 ...
gi 313199514 222 VTQ 224
Cdd:cd14601  169 LIE 171
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 70-224 8.54e-08

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: 51.77  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  70 KYICISDPKAENYEKFWELAWCREVNTIV---KISQREEESC-QYWSSREgSEIECGGFRIK------TLIVIKRprfis 139
Cdd:cd14600   83 KYIATQGPLPHTCAQFWQVVWEQKLSLIVmltTLTERGRTKChQYWPDPP-DVMEYGGFRVQchsedcTIAYVFR----- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 140 TLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVcslndTYTTSKKEQSAewklgTVLVHCNDGSSFSAVYCVLD 219
Cdd:cd14600  157 EMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFV-----NYVRSKRVENE-----PVLVHCSAGIGRTGVLVTME 226


                 ....*..
gi 313199514 220 --MCVTQ 224
Cdd:cd14600  227 taMCLTE 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 53-241 1.57e-07

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 50.69  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SCQYWSSREGSEIECGGFRIKTL 129
Cdd:cd14617   27 YINASYIPGNNF---RREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgrvKCDHYWPADQDSLYYGDLIVQML 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 130 IVIKRPRF-ISTLLLLS-DQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEqsaewklGTVLVHCND 207
Cdd:cd14617  104 SESVLPEWtIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRTPGS-------GPTVVHCSA 176

                        170       180       190
                 ....*....|....*....|....*....|....
gi 313199514 208 GSSFSAVYCVLDMCVTQFKYTGTISVANAYRKIK 241
Cdd:cd14617  177 GVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLR 210
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 53-219 1.70e-07

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: 50.11  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVkISQREEES----CQ-YWSSREGSEIECGGFRIk 127
Cdd:cd14542    1 YINANFIKGVSG---SKAYIATQGPLPNTVLDFWRMIWEYNVQVIV-MACREFEMgkkkCErYWPEEGEEQLQFGPFKI- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKR--PRFISTLLLLSDQKNrKREILHYHYTASPTNNNSDEPFIFLSFVcSLNDTYTTSKKEqsaewklgTVLVHC 205
Cdd:cd14542   76 SLEKEKRvgPDFLIRTLKVTFQKE-SRTVYQFHYTAWPDHGVPSSVDPILDLV-RLVRDYQGSEDV--------PICVHC 145

                        170
                 ....*....|....
gi 313199514 206 NDGSSFSAVYCVLD 219
Cdd:cd14542  146 SAGCGRTGTICAID 159
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 53-240 2.52e-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: 49.61  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQRE---EESCQYWSSREgSEIECGGFRIKTL 129
Cdd:cd17669    1 YINASYIMGYY---QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQnmaEDEFVYWPNKD-EPINCETFKVTLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 130 ------IVIKRPRFISTLLLLSDQKNRKREILHYHYTASPtnnNSDEP----FIFLSFVcslndtyttskKEQSAEwKLG 199
Cdd:cd17669   77 aeehkcLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWP---NPDSPisktFELISII-----------KEEAAN-RDG 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 313199514 200 TVLVHCNDGSSFSAVYCVLDMCVTQFKYTGTISVANAYRKI 240
Cdd:cd17669  142 PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMI 182
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 53-219 2.84e-07

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: 50.41  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDaydRQRKYICISDPKAENYEKFWELAWCREVNTIVKIS---QREEESC-QYWSSRegseiEC---GGFR 125
Cdd:cd14621   82 YINASFINGYQ---EKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTnlkERKECKCaQYWPDQ-----GCwtyGNIR 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 126 IK---TLIVIKRPRFISTLLLLSDQKNRK--REILHYHYTASPTNNNSDEPFIFLSF---VCSLNDTYTtskkeqsaewk 197
Cdd:cd14621  154 VSvedVTVLVDYTVRKFCIQQVGDVTNKKpqRLITQFHFTSWPDFGVPFTPIGMLKFlkkVKNCNPQYA----------- 222

                        170       180
                 ....*....|....*....|..
gi 313199514 198 lGTVLVHCNDGSSFSAVYCVLD 219
Cdd:cd14621  223 -GAIVVHCSAGVGRTGTFIVID 243
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 53-242 4.76e-07

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: 49.12  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SCQYWSSREGSEIECGGFRIKTL 129
Cdd:cd14619   27 YINANYMPGYWS---SQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAgrvKCEHYWPLDYTPCTYGHLRVTVV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 130 IVIKRPRF-ISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVcSLNDTYTTSKKEQsaewklGTVLVHCNDG 208
Cdd:cd14619  104 SEEVMENWtVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFR-RLLRQWLDQTMSG------GPTVVHCSAG 176

                        170       180       190
                 ....*....|....*....|....*....|....
gi 313199514 209 SSFSAVYCVLDMCVTQFKYTGTISVANAYRKIKQ 242
Cdd:cd14619  177 VGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRE 210
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 71-243 4.98e-07

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: 49.61  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  71 YICISDPKAENYEKFWELAWCREVNTIVKISQREEE----SCQYW---SSREGSEIEcGGFRIKTLIVIKRPRFISTLL- 142
Cdd:cd14599   84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGgrskSHRYWpklGSKHSSATY-GKFKVTTKFRTDSGCYATTGLk 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 143 ---LLSDQknrKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDT--YTTSKKEQSAEWKlGTVLVHCNDGSSFSAVYCV 217
Cdd:cd14599  163 vkhLLSGQ---ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrHTNSMLDSTKNCN-PPIVVHCSAGVGRTGVVIL 238

                        170       180
                 ....*....|....*....|....*.
gi 313199514 218 LDMCVTQFKYTGTISVANAYRKIKQR 243
Cdd:cd14599  239 TELMIGCLEHNEKVEVPVMLRHLREQ 264
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 70-208 5.06e-07

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: 48.86  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  70 KYICISDPKAENYEKFWELAWCREVNTIVKIS---QREEESC-QYWsSREGSEIECGGFRIKTLIVIKRPRFISTLLLLS 145
Cdd:cd14541   20 RYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTtlvERGRVKChQYW-PDLGETMQFGNLQITCVSEEVTPSFAFREFILT 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313199514 146 D-QKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLndtyttskkEQSAEWKLGTVLVHCNDG 208
Cdd:cd14541   99 NtNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV---------RQNRVGMVEPTVVHCSAG 153
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 55-224 2.15e-06

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: 47.74  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  55 RADFIDGYDAYD---RQRKYICISDPKAENYEKFWELAW---CREVNTIVKISQREEESC-QYWSSrEGSEIecggFRIK 127
Cdd:cd14610   71 HSDYINASPIMDhdpRNPAYIATQGPLPATVADFWQMVWesgCVVIVMLTPLAENGVKQCyHYWPD-EGSNL----YHIY 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKR-----PRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYttskKEQSAewklgTVL 202
Cdd:cd14610  146 EVNLVSEhiwceDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCY----RGRSC-----PII 216

                        170       180
                 ....*....|....*....|..
gi 313199514 203 VHCNDGSSFSAVYCVLDMCVTQ 224
Cdd:cd14610  217 VHCSDGAGRSGTYILIDMVLNK 238
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 53-219 3.46e-06

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: 47.23  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVkISQREEE----SCQ-YWSSREGSEIECGGFRIK 127
Cdd:cd14604   87 YINANFIKGVYG---PKAYIATQGPLANTVIDFWRMIWEYNVAIIV-MACREFEmgrkKCErYWPLYGEEPMTFGPFRIS 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TliVIKRPR---FISTLLLlsDQKNRKREILHYHYTASPtnnNSDEPFIFLSFVcslnDTYTTSKKEQSAEWKlgTVLVH 204
Cdd:cd14604  163 C--EAEQARtdyFIRTLLL--EFQNETRRLYQFHYVNWP---DHDVPSSFDSIL----DMISLMRKYQEHEDV--PICIH 229

                        170
                 ....*....|....*
gi 313199514 205 CNDGSSFSAVYCVLD 219
Cdd:cd14604  230 CSAGCGRTGAICAID 244
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 68-222 3.82e-06

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: 46.80  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  68 QRKYICISDPKAENYEKFWELAWcREVNTIVKISQREEESCQ-----YWSSrEGSEIECGGFRIKTLIVIKRPRFISTLL 142
Cdd:cd14606   66 AKTYIASQGCLEATVNDFWQMAW-QENSRVIVMTTREVEKGRnkcvpYWPE-VGMQRAYGPYSVTNCGEHDTTEYKLRTL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 143 LLS--DQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNdtyttskKEQSAEWKLGTVLVHCNDGSSFSAVYCVLDM 220
Cdd:cd14606  144 QVSplDNGELIREIWHYQYLSWPDHGVPSEPGGVLSFLDQIN-------QRQESLPHAGPIIVHCSAGIGRTGTIIVIDM 216


                 ..
gi 313199514 221 CV 222
Cdd:cd14606  217 LM 218
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 66-214 1.07e-05

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: 44.97  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  66 DRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQRE----EESCQYWsSREGSE---IECGGFRIKTLIVIKRPRFI 138
Cdd:cd14598   13 GKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEeggrEKSFRYW-PRLGSRhntVTYGRFKITTRFRTDSGCYA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 139 STLL----LLSDQknrKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTSKKEQSAEWKLGTVLVHCNDGSSFSAV 214
Cdd:cd14598   92 TTGLkikhLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLVHCSAGVGRTGV 168
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 53-219 1.50e-05

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: 44.88  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYDAydrQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SC-QYWSSREgSEIECGGFRIKT 128
Cdd:cd14614   42 YINANYIPGYNS---PQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKrrvKCdHYWPFTE-EPVAYGDITVEM 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSdQKNRKREILHYHYTASPTNN--NSDEPFIFLSFVCSLNDTYTTSKkeqsaewklGTVLVHCN 206
Cdd:cd14614  118 LSEEEQPDWAIREFRVS-YADEVQDVMHFNYTAWPDHGvpTANAAESILQFVQMVRQQAVKSK---------GPMIIHCS 187

                        170
                 ....*....|...
gi 313199514 207 DGSSFSAVYCVLD 219
Cdd:cd14614  188 AGVGRTGTFIALD 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 55-243 2.63e-05

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: 44.26  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  55 RADFIDGYDAYD---RQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEE---SC-QYWSSrEGSEIecggFRIK 127
Cdd:cd14609   69 RSDYINASPIIEhdpRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDgvkQCdRYWPD-EGSSL----YHIY 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIK-----RPRFISTLLLLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYttskKEQSAewklgTVL 202
Cdd:cd14609  144 EVNLVSehiwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY----RGRSC-----PII 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313199514 203 VHCNDGSSFSAVYCVLDMCVTQF-KYTGTISVANAYRKIK-QR 243
Cdd:cd14609  215 VHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRdQR 257
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 53-220 4.02e-05

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: 43.16  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDGYdaydRQRK-YICISDPKAENYEKFWELAWCREVNTIVKISQ--REEESC-QYWSSREGSEIecGGFRIKT 128
Cdd:cd14556    1 YINAALLDSY----KQPAaFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQldPKDQSCpQYWPDEGSGTY--GPIQVEF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 129 LIVIKRPRFISTLLLLSDQKNRKREIL---HYHYTASPTNNNS-DEPFIFLSFVCSLndtytTSKKEQSAEwklGTVLVH 204
Cdd:cd14556   75 VSTTIDEDVISRIFRLQNTTRPQEGYRmvqQFQFLGWPRDRDTpPSKRALLKLLSEV-----EKWQEQSGE---GPIVVH 146

                        170
                 ....*....|....*.
gi 313199514 205 CNDGSSFSAVYCVLDM 220
Cdd:cd14556  147 CLNGVGRSGVFCAISS 162
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 68-245 3.54e-04

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: 40.50  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  68 QRKYICISDPKAENYEKFWELAWCREVNTIVKISQREE----ESCQYWSSREGSEIECGGFRIKTLIVIKRPRF-ISTLL 142
Cdd:cd14596   15 ELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVErgkvKCHRYWPETLQEPMELENYQLRLENYQALQYFiIRIIK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 143 LLSDQKNRKREILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTskkeqsaewklGTVLVHCNDGSSFSAVYCVLDMCV 222
Cdd:cd14596   95 LVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT-----------GPIVVHCSAGIGRAGVLICVDVLL 163

                        170       180
                 ....*....|....*....|...
gi 313199514 223 TQFKYTGTISVANAYRKIKQREH 245
Cdd:cd14596  164 SLIEKDLSFNIKDIVREMRQQRY 186
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 53-208 5.13e-04

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: 40.05  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514  53 YLRADFIDgYDAYDRQRKYICISDPKAENYEKFWELAWCREVNTIVKISQREEES---C-QYWSSREGSEIECGG-FRIK 127
Cdd:cd14538    1 YINASHIR-IPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGkvkChRYWPDSLNKPLICGGrLEVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313199514 128 TLIVIKRPRFISTLLLLSDQKNRK-REILHYHYTASPTNNNSDEPFIFLSFVCSLNDTYTTskkeqsaewklGTVLVHCN 206
Cdd:cd14538   80 LEKYQSLQDFVIRRISLRDKETGEvHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS-----------GPIVVHCS 148


                 ..
gi 313199514 207 DG 208
Cdd:cd14538  149 AG 150
 
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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