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Conserved domains on  [gi|6679553|ref|NP_033003|]
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tyrosine-protein phosphatase non-receptor type 2 isoform a [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 19-272 0e+00

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


The actual alignment was detected with superfamily member cd14607:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 257  Bit Score: 538.78  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607   1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   99 LMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHY 177
Cdd:cd14607  81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  178 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYR 255
Cdd:cd14607 161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                       250
                ....*....|....*..
gi 6679553  256 MGLIQTPDQLRFSYMAI 272
Cdd:cd14607 241 MGLIQTPDQLRFSYMAV 257
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-272 0e+00

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: 538.78  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607   1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   99 LMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHY 177
Cdd:cd14607  81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  178 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYR 255
Cdd:cd14607 161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                       250
                ....*....|....*..
gi 6679553  256 MGLIQTPDQLRFSYMAI 272
Cdd:cd14607 241 MGLIQTPDQLRFSYMAV 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-274 3.83e-111

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 324.58  E-value: 3.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     42 NRNRNRYRDVSPYDHSRVKLQSTE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    120 SVKCAQYWPT-DDREMVFKetGFSVKLLSE-DVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLF 197
Cdd:pfam00102  81 REKCAQYWPEeEGESLEYG--DFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553    198 KVRESgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-274 1.18e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 321.53  E-value: 1.18e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553       5 IEREFEELDaqcrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTE---NDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553      82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKetGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     161 LENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE 240
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 6679553     241 DVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-277 1.68e-50

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 171.34  E-value: 1.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    41 ENRNRNRYRDVSPYDHSRVKLQSTE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEK 118
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   119 ESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKS--YYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFL 196
Cdd:PHA02742 131 GKEACYPYWMPHERGKA---THGEFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   197 FKVRESGCLT--PDHG-------PAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:PHA02742 208 LAVREADLKAdvDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287

                        250
                 ....*....|
gi 6679553   268 SYMAIIEGAK 277
Cdd:PHA02742 288 CYFIVLIFAK 297
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-265 1.64e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.46  E-value: 1.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   40 PENRNRNRYRDVSPYDHSRVklqsTEND-YINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVE- 117
Cdd:COG5599  40 INGSPLNRFRDIQPYKETAL----RANLgYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEi 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  118 -KESVKCAQYWPTDDREMVFKetgFSVKLL-SEDVKSYYTVHLLQLENINTG-ETRTISHFHYTTWPDFGVPESPAsFLN 194
Cdd:COG5599 115 sKPKVKMPVYFRQDGEYGKYE---VSSELTeSIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAEA-LKN 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679553  195 FLFKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLvdtCLVLM-----EKGEDVNVKQLLLNMRKYR-MGLIQTPDQL 265
Cdd:COG5599 191 LADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSksinaLVQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
 
Name Accession Description Interval E-value
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 19-272 0e+00

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: 538.78  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   19 QPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFW 98
Cdd:cd14607   1 QPLYLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   99 LMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDD-REMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHY 177
Cdd:cd14607  81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  178 TTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEK--GEDVNVKQLLLNMRKYR 255
Cdd:cd14607 161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKkdPDSVDIKQVLLDMRKYR 240

                       250
                ....*....|....*..
gi 6679553  256 MGLIQTPDQLRFSYMAI 272
Cdd:cd14607 241 MGLIQTPDQLRFSYMAV 257
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 18-290 5.59e-175

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: 488.00  E-value: 5.59e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   18 WQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14608   1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   98 WLMVWQQKTKAVVMLNRTVEKESVKCAQYWP-TDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFH 176
Cdd:cd14608  81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPqKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  177 YTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED---VNVKQLLLNMRK 253
Cdd:cd14608 161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDpssVDIKKVLLEMRK 240

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6679553  254 YRMGLIQTPDQLRFSYMAIIEGAKYTKGDSNIQKRWK 290
Cdd:cd14608 241 FRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWK 277
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 43-270 2.46e-159

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: 446.45  E-value: 2.46e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   43 RNRNRYRDVSPYDHSRVKLQSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVK 122
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  123 CAQYWPTDDRE-MVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 201
Cdd:cd14545  81 CAQYWPQGEGNaMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679553  202 SGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE--DVNVKQLLLNMRKYRMGLIQTPDQLRFSYM 270
Cdd:cd14545 161 SGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSYL 231
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
42-274 3.83e-111

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 324.58  E-value: 3.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     42 NRNRNRYRDVSPYDHSRVKLQSTE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKE 119
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPgpSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    120 SVKCAQYWPT-DDREMVFKetGFSVKLLSE-DVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLF 197
Cdd:pfam00102  81 REKCAQYWPEeEGESLEYG--DFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553    198 KVRESgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
5-274 1.18e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 321.53  E-value: 1.18e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553       5 IEREFEELDaqcrwqplyleiRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTE---NDYINASLVDIEEAQR 81
Cdd:smart00194   2 LEEEFEKLD------------RLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGPK 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553      82 SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKetGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:smart00194  70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYG--DITVTLKSVEKVDDYTIRTLE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     161 LENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE 240
Cdd:smart00194 148 VTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                          250       260       270
                   ....*....|....*....|....*....|....
gi 6679553     241 DVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:smart00194 226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 68-270 9.22e-86

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: 258.75  E-value: 9.22e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdrEMVFKETG-FSVKLL 146
Cdd:cd00047   1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEE--GGKPLEYGdITVTLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTF 226
Cdd:cd00047  79 SEEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6679553  227 SLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYM 270
Cdd:cd00047 157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 22-270 8.92e-83

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: 253.44  E-value: 8.92e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQS----TENDYINASLVDIEEAQRSYILTQGPLPNTCCHF 97
Cdd:cd14543   9 YEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKrngdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   98 WLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTD-DREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFH 176
Cdd:cd14543  89 WRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEeGSSLRYGD--LTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQ 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  177 YTTWPDFGVPESPASFLNFLFKVRE---SGCLT--------PDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVK 245
Cdd:cd14543 167 FTSWPDFGVPSSAAALLDFLGEVRQqqaLAVKAmgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVM 246

                       250       260
                ....*....|....*....|....*
gi 6679553  246 QLLLNMRKYRMGLIQTPDQLRFSYM 270
Cdd:cd14543 247 QTVRRMRTQRAFSIQTPDQYYFCYK 271
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 42-276 2.62e-77

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: 238.45  E-value: 2.62e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   42 NRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVE 117
Cdd:cd14553   3 NKPKNRYANVIAYDHSRVILQPIEgvpgSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  118 KESVKCAQYWPTDDREmvfKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLF 197
Cdd:cd14553  83 RSRVKCDQYWPTRGTE---TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679553  198 KVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEGA 276
Cdd:cd14553 160 RVK--ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 47-267 3.12e-71

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: 222.23  E-value: 3.12e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   47 RYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVK 122
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINeeegSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  123 CAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENIntGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 202
Cdd:cd14548  81 CDHYWPFDQDPVYYGD--ITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  203 gcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14548 157 --IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 37-273 7.60e-69

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: 218.18  E-value: 7.60e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   37 AKFPENRNRNRYRDVSPYDHSRVKLQSTEnDYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14600  35 AKLPQNMDKNRYKDVLPYDATRVVLQGNE-DYINASYVNMEIPSANivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVML 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  113 NRTVEKESVKCAQYWPtdDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASF 192
Cdd:cd14600 114 TTLTERGRTKCHQYWP--DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDF 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  193 LNFLFKVREsgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14600 192 LEFVNYVRS---KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268


                .
gi 6679553  273 I 273
Cdd:cd14600 269 L 269
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 68-274 5.64e-68

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: 213.39  E-value: 5.64e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETGFSVKL 145
Cdd:cd14538   1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICGGRLEVSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  146 LSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGcltpDHGPAVIHCSAGIGRSGT 225
Cdd:cd14538  81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH----NSGPIVVHCSAGIGRTGV 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6679553  226 FSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14538 157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 42-272 6.34e-66

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: 209.63  E-value: 6.34e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   42 NRNRNRYRDVSPYDHSRVKLQSTEN-----DYINASLVDIEEAQR-------SYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDRDPnvpgsDYINANYIRNENEGPttdenakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  110 VMLNRTVEKESVKCAQYWPtdDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGE-TRTISHFHYTTWPDFGVPES 188
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWP--DEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDpIREIWHYQYLSWPDHGVPSD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  189 PASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGED--VNVKQLLLNMRKYRMGLIQTPDQL 265
Cdd:cd14544 159 PGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLdQIKRKGLDcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                ....*..
gi 6679553  266 RFSYMAI 272
Cdd:cd14544 239 KFIYVAV 245
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 67-273 1.68e-65

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: 207.18  E-value: 1.68e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   67 DYINASLVDIE----EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFS 142
Cdd:cd14541   1 DYINANYVNMEipgsGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFG--NLQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  143 VKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR--ESGCLTpdhgPAVIHCSAGI 220
Cdd:cd14541  79 ITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRqnRVGMVE----PTVVHCSAGI 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6679553  221 GRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd14541 155 GRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 46-267 3.45e-65

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: 206.98  E-value: 3.45e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKL---QSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVK 122
Cdd:cd14615   1 NRYNNVLPYDISRVKLsvqSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  123 CAQYWPTDDREMVfkeTGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 202
Cdd:cd14615  81 CEEYWPSKQKKDY---GDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  203 GCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14615 158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 68-267 6.91e-65

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: 205.28  E-value: 6.91e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfkETG-FSVKLL 146
Cdd:cd14549   1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE----TYGnIQVTLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENIN------TGETRTISHFHYTTWPDFGVPESPASFLNFLFKVreSGCLTPDHGPAVIHCSAGI 220
Cdd:cd14549  77 STEVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS--SAANPPGAGPIVVHCSAGV 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6679553  221 GRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14549 155 GRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 41-272 2.24e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 203.33  E-value: 2.24e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   41 ENRNRNRYRDVSPYDHSRVKLQSTE-----NDYINASLVDIE--------EAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDpnepvSDYINANIIMPEfetkcnnsKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  108 AVVMLNRTVEKESVKCAQYWPTddrEMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHYTTWPDFGV 185
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWPD---EYALKEYGvMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  186 PESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCL-VLMEKGE--DVNVKQLLLNMRKYRMGLIQTP 262
Cdd:cd14605 158 PSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIdIIREKGVdcDIDVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|
gi 6679553  263 DQLRFSYMAI 272
Cdd:cd14605 238 AQYRFIYMAV 247
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 46-267 8.94e-62

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: 198.00  E-value: 8.94e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKLQSTEND----YINASLV---DIEEaqRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEK 118
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIrgyDGEE--KAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  119 EsVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENinTGETRTISHFHYTTWPDFGVPESPASFLNFLFK 198
Cdd:cd14547  79 K-EKCAQYWPE---EENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQE 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  199 VRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGEdVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14547 153 VEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 7-276 1.01e-61

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: 199.88  E-value: 1.01e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    7 REFEELD--AQCRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQ 80
Cdd:cd14626  20 QEYESIDpgQQFTWENSNLEV----------------NKPKNRYANVIAYDHSRVILTSVDgvpgSDYINANYIDGYRKQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:cd14626  84 NAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETY---GMIQVTLLDTVELATYSVRTFA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  161 LENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE 240
Cdd:cd14626 161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK 238

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 6679553  241 DVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEGA 276
Cdd:cd14626 239 TVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 41-273 3.39e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 196.97  E-value: 3.39e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   41 ENRNRNRYRDVSPYDHSRVKLqSTENDYINASLVDIEEAQRS--YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEK 118
Cdd:cd14597   2 ENRKKNRYKNILPYDTTRVPL-GDEGGYINASFIKMPVGDEEfvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  119 ESVKCAQYWPTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFK 198
Cdd:cd14597  81 GKIKCQRYWPEILGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFISY 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  199 VREsgclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd14597 161 MRH----IHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 46-270 2.06e-60

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: 194.75  E-value: 2.06e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKLQSTEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESV 121
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  122 KCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHYTTWPDFGVPESPASFLNFLFKVR 200
Cdd:cd14617  81 KCDHYWPADQDSLYYGD--LIVQMLSESVLPEWTIREFKICSEEQLDApRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  201 ESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQlrFSYM 270
Cdd:cd14617 159 DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQ--YVYL 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 40-274 2.59e-60

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: 195.87  E-value: 2.59e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   40 PENRNRNRYRDVSPYDHSRVKLQSTEN-----DYINAS-----LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 109
Cdd:cd14606  16 PENKSKNRYKNILPFDHSRVILQGRDSnipgsDYINANyvknqLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  110 VMLNRTVEKESVKCAQYWPTDDREmvfKETG-FSVKLLSEDVKSYYTVHLLQLENINTGET-RTISHFHYTTWPDFGVPE 187
Cdd:cd14606  96 VMTTREVEKGRNKCVPYWPEVGMQ---RAYGpYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  188 SPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLME-KG--EDVNVKQLLLNMRKYRMGLIQTPDQ 264
Cdd:cd14606 173 EPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIStKGldCDIDIQKTIQMVRAQRSGMVQTEAQ 252

                       250
                ....*....|
gi 6679553  265 LRFSYMAIIE 274
Cdd:cd14606 253 YKFIYVAIAQ 262
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 40-274 3.39e-60

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 195.64  E-value: 3.39e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   40 PENRNRNRYRDVSPYDHSRVKLQ------STENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd17667  25 PDNKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  114 RTVEKESVKCAQYWPTDDREmvfkETG-FSVKLLSEDVKSYYTVHLLQLENINTGE-----------TRTISHFHYTTWP 181
Cdd:cd17667 105 NLVEKGRRKCDQYWPTENSE----EYGnIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkgnpkgrqnERTVIQYHYTQWP 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  182 DFGVPESPASFLNFLfkVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQT 261
Cdd:cd17667 181 DMGVPEYALPVLTFV--RRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQT 258

                       250
                ....*....|...
gi 6679553  262 PDQLRFSYMAIIE 274
Cdd:cd17667 259 EEQYIFIHDALLE 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 31-267 6.48e-60

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: 193.95  E-value: 6.48e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   31 DYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTEN----DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 106
Cdd:cd14614   1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEeegsDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  107 KAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYTTWPDFGVP 186
Cdd:cd14614  81 QIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGD--ITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  187 ESPA--SFLNFLFKVRESGCLTPdhGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQ 264
Cdd:cd14614 157 TANAaeSILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQ 234


                ...
gi 6679553  265 LRF 267
Cdd:cd14614 235 YIF 237
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 46-274 1.56e-58

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: 190.10  E-value: 1.56e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKL----QSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESV 121
Cdd:cd14619   1 NRFRNVLPYDWSRVPLkpihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  122 KCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 201
Cdd:cd14619  81 KCEHYWPLDYTPCTYGH--LRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679553  202 SGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14619 159 WLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 2-275 2.20e-58

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 191.46  E-value: 2.20e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    2 SATIEREFEELDA--QCRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVD 75
Cdd:cd14625  21 NLKLSQEYESIDPgqQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVILQPIEgimgSDYINANYID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   76 IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVfketGF-SVKLLSEDVKSYY 154
Cdd:cd14625  85 GYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETY----GMiQVTLLDTIELATF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  155 TVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLV 234
Cdd:cd14625 161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT--CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLE 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 6679553  235 LMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEG 275
Cdd:cd14625 239 RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 36-274 1.75e-57

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: 189.11  E-value: 1.75e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   36 VAKFPENRNRNRYRDVSPYDHSRVKLQSTEN----DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14610  38 VAQREENVQKNRSLAVLPYDHSRIILKAENShshsDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIV 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  111 MLNRTVEKESVKCAQYWPTDDREMVFKetgFSVKLLSED-------VKSYYtvhllqLENINTGETRTISHFHYTTWPDF 183
Cdd:cd14610 118 MLTPLAENGVKQCYHYWPDEGSNLYHI---YEVNLVSEHiwcedflVRSFY------LKNLQTNETRTVTQFHFLSWNDQ 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  184 GVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRKYRMGLIQTP 262
Cdd:cd14610 189 GVPASTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTK 266

                       250
                ....*....|..
gi 6679553  263 DQLRFSYMAIIE 274
Cdd:cd14610 267 EQFEFALTAVAE 278
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 8-274 8.71e-57

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: 186.57  E-value: 8.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    8 EFEELDAQC-RWQplyleirnESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQST----ENDYINASLVDIEEAQRS 82
Cdd:cd14603   3 EFSEIRACSaAFK--------ADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLqeegHSDYINANFIKGVDGSRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   83 YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVhLLQLE 162
Cdd:cd14603  75 YIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGP--FTITLVKEKRLNEEVI-LRTLK 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  163 NINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDhgPAVIHCSAGIGRSGTFSLVDTC--LVLMEK-G 239
Cdd:cd14603 152 VTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDYVrqLLLTQRiP 229

                       250       260       270
                ....*....|....*....|....*....|....*
gi 6679553  240 EDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14603 230 PDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 68-269 2.06e-56

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: 183.60  E-value: 2.06e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEA-QRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFSVKLL 146
Cdd:cd18533   1 YINASYITLPGTsSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYG--DLTVELV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDV--KSYYTVHLLQLeNINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSG 224
Cdd:cd18533  79 SEEEndDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  225 TFSLVDTCLVLMEKG----------EDVnVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd18533 158 TFIALDSLLDELKRGlsdsqdledsEDP-VYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 7-275 1.30e-55

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 184.16  E-value: 1.30e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    7 REFEELDA--QCRWQPLYLEIrneshdyphrvakfpeNRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQ 80
Cdd:cd14624  26 QEYESIDPgqQFTWEHSNLEV----------------NKPKNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   81 RSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfKETGFSVKLLSEDVKSYYTVHLLQ 160
Cdd:cd14624  90 NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE---TYGLIQVTLLDTVELATYCVRTFA 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  161 LENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGE 240
Cdd:cd14624 167 LYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT--CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK 244

                       250       260       270
                ....*....|....*....|....*....|....*
gi 6679553  241 DVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEG 275
Cdd:cd14624 245 TVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEA 279
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 68-274 1.35e-55

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: 181.48  E-value: 1.35e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIE--EAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKL 145
Cdd:cd14596   1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWP-ETLQEPMELENYQLRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  146 LSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLtpdhGPAVIHCSAGIGRSGT 225
Cdd:cd14596  80 ENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT----GPIVVHCSAGIGRAGV 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6679553  226 FSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14596 156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 36-274 1.67e-55

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: 183.70  E-value: 1.67e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   36 VAKFPENRNRNRYRDVSPYDHSRVKLQSTEN----DYINAS-LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 110
Cdd:cd14609  36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIV 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  111 MLNRTVEKESVKCAQYWPTDDREM--VFKETGFSVKLLSED--VKSYYtvhllqLENINTGETRTISHFHYTTWPDFGVP 186
Cdd:cd14609 116 MLTPLVEDGVKQCDRYWPDEGSSLyhIYEVNLVSEHIWCEDflVRSFY------LKNVQTQETRTLTQFHFLSWPAEGIP 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  187 ESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRKYRMGLIQTPDQL 265
Cdd:cd14609 190 SSTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGMVRTKDQF 267


                ....*....
gi 6679553  266 RFSYMAIIE 274
Cdd:cd14609 268 EFALTAVAE 276
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 67-274 3.82e-55

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: 180.53  E-value: 3.82e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   67 DYINASLVDIEEAQRS----YILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetGFS 142
Cdd:cd14601   1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYG--GFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  143 VKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDhgPAVIHCSAGIGR 222
Cdd:cd14601  79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679553  223 SGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14601 157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 68-274 4.34e-55

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: 180.33  E-value: 4.34e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKetgFSVKLL 146
Cdd:cd14546   1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI---YEVHLV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKS-YYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES----GCltpdhgPAVIHCSAGIG 221
Cdd:cd14546  78 SEHIWCdDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSyrgrSC------PIVVHCSDGAG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679553  222 RSGTFSLVDTCLVLMEKG-EDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14546 152 RTGTYILIDMVLNRMAKGaKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 46-273 1.64e-54

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: 179.37  E-value: 1.64e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKL----QSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESV 121
Cdd:cd14618   1 NRYPHVLPYDHSRVRLsqlgGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  122 KCAQYWPTDDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE 201
Cdd:cd14618  81 LCDHYWPSESTPVSYGH--ITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679553  202 SGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd14618 159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 37-271 2.51e-54

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 179.26  E-value: 2.51e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   37 AKFPENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14554   1 ANLPCNKFKNRLVNILPYESTRVCLQPIRgvegSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  113 NRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASF 192
Cdd:cd14554  81 TKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGF 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679553  193 LNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMA 271
Cdd:cd14554 158 IDFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 32-272 1.47e-53

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: 179.36  E-value: 1.47e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   32 YPHRVAKFPENRNRNRYRDVSPYDHSRVKL----QSTENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 107
Cdd:cd14604  47 YPTATGEKEENVKKNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  108 AVVMLNRTVEKESVKCAQYWPT-DDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYTTWPDFGVP 186
Cdd:cd14604 127 IIVMACREFEMGRKKCERYWPLyGEEPMTFGP--FRISCEAEQARTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVP 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  187 ESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKG---EDVNVKQLLLNMRKYRMGLIQTPD 263
Cdd:cd14604 203 SSFDSILDMISLMRKYQ--EHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGkipEEFNVFNLIQEMRTQRHSAVQTKE 280


                ....*....
gi 6679553  264 QLRFSYMAI 272
Cdd:cd14604 281 QYELVHRAI 289
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 41-275 1.50e-53

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: 177.14  E-value: 1.50e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   41 ENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTV 116
Cdd:cd14630   2 ENRNKNRYGNIISYDHSRVRLQLLDgdphSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  117 EKESVKCAQYWPtDDREmVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFL 196
Cdd:cd14630  82 EVGRVKCVRYWP-DDTE-VYGD--IKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679553  197 FKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEG 275
Cdd:cd14630 158 RQVKFLN--PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEA 234
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 68-274 1.69e-53

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: 176.49  E-value: 1.69e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEE--AQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETG-FSVK 144
Cdd:cd14540   1 YINASHITATVggKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFGeYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  145 LLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRE-----SGCLTPD--HGPAVIHCS 217
Cdd:cd14540  81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtNQDVAGHnrNPPTLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553  218 AGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 28-275 1.14e-52

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: 176.39  E-value: 1.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   28 ESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQ 103
Cdd:cd14633  26 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEgetsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  104 QKTKAVVMLNRTVEKESVKCAQYWPtDDREmVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDF 183
Cdd:cd14633 106 ENTASIIMVTNLVEVGRVKCCKYWP-DDTE-IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDH 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  184 GVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPD 263
Cdd:cd14633 182 GVPYHATGLLGFVRQVKSKS--PPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEE 259

                       250
                ....*....|..
gi 6679553  264 QLRFSYMAIIEG 275
Cdd:cd14633 260 QYVFIHDAILEA 271
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 48-274 1.14e-52

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: 174.74  E-value: 1.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   48 YRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKC 123
Cdd:cd14620   1 YPNILPYDHSRVILSQLDgipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  124 AQYWPtDDREMVFKetgfSVKLLSED--VKSYYTVHLLQLENINTGET---RTISHFHYTTWPDFGVPESPASFLNFLFK 198
Cdd:cd14620  81 YQYWP-DQGCWTYG----NIRVAVEDcvVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553  199 VREsgcLTPDH-GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14620 156 VKS---VNPVHaGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 41-285 2.09e-51

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: 173.67  E-value: 2.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   41 ENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTV 116
Cdd:cd14621  51 ENKEKNRYVNILPYDHSRVHLTPVEgvpdSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  117 EKESVKCAQYWPtDDREMVFKETGFSVkllsEDVKSY--YTVHLLQLENI----NTGETRTISHFHYTTWPDFGVPESPA 190
Cdd:cd14621 131 ERKECKCAQYWP-DQGCWTYGNIRVSV----EDVTVLvdYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPI 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  191 SFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYM 270
Cdd:cd14621 206 GMLKFLKKVK--NCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQ 283

                       250
                ....*....|....*
gi 6679553  271 AIIEgaKYTKGDSNI 285
Cdd:cd14621 284 ALLE--HYLYGDTEL 296
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 45-274 2.80e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 171.18  E-value: 2.80e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   45 RNRYRDVSPYDHSRVKLQ----STENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKES 120
Cdd:cd14602   1 KNRYKDILPYDHSRVELSlitsDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  121 VKCAQYWpTDDREMVFKETGFSVKLLSEDVKSYYTVHLLQLENINtgETRTISHFHYTTWPDFGVPESPASFLNFLFKVR 200
Cdd:cd14602  81 KKCERYW-AEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679553  201 esgCLTPDHG-PAVIHCSAGIGRSGTFSLVDTCLVLMEKG---EDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14602 158 ---CYQEDDSvPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 68-269 1.19e-50

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: 168.72  E-value: 1.19e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTdDREMVFKETGFSVKLL 146
Cdd:cd14539   1 YINASLIeDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPT-ERGQALVYGAITVSLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLT-PDHGPAVIHCSAGIGRSGT 225
Cdd:cd14539  80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6679553  226 FSLVDTCLVLMEKG-EDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14539 160 FCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 41-277 1.68e-50

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 171.34  E-value: 1.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    41 ENRNRNRYRDVSPYDHSRVKLQSTE--NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEK 118
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILKIEDggDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   119 ESVKCAQYWPTDDREMVfkeTGFSVKLLSEDVKS--YYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFL 196
Cdd:PHA02742 131 GKEACYPYWMPHERGKA---THGEFKIKTKKIKSfrNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   197 FKVRESGCLT--PDHG-------PAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:PHA02742 208 LAVREADLKAdvDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287

                        250
                 ....*....|
gi 6679553   268 SYMAIIEGAK 277
Cdd:PHA02742 288 CYFIVLIFAK 297
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 46-267 4.27e-50

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


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 167.78  E-value: 4.27e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESV 121
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAgvpgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  122 KCAQYWPTDDREM-VFKEtgFSVKLLSEDVKSYYTVHLLQLEniNTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVR 200
Cdd:cd14616  81 RCHQYWPEDNKPVtVFGD--IVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553  201 ESgcLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14616 157 AS--RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 22-274 4.39e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 169.79  E-value: 4.39e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   22 YLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQST-END--YINAS--LVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:cd14599  18 YEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTkENNtgYINAShiKVTVGGEEWHYIATQGPLPHTCHD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   97 FWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREMVFKETG-FSVKLLSEDVKSYYTVHLLQLENINTGETRTISHF 175
Cdd:cd14599  98 FWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKHSSATYGkFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHL 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  176 HYTTWPDFGVPESPASFLNFLFKVRE-----------SGCLTPdhgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNV 244
Cdd:cd14599 178 QYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldsTKNCNP---PIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEV 254

                       250       260       270
                ....*....|....*....|....*....|
gi 6679553  245 KQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14599 255 PVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 37-274 2.42e-48

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


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 165.68  E-value: 2.42e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   37 AKFPENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14628  47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  113 NRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASF 192
Cdd:cd14628 127 TKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGF 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  193 LNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14628 204 IDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAA 283


                ..
gi 6679553  273 IE 274
Cdd:cd14628 284 LE 285
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 68-273 2.50e-48

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: 162.84  E-value: 2.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREmvfkETG-FSVKLL 146
Cdd:cd17668   1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE----EYGnFLVTQK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLEN--INTG------ETRTISHFHYTTWPDFGVPESPASFLNFLFKvrESGCLTPDHGPAVIHCSA 218
Cdd:cd17668  77 SVQVLAYYTVRNFTLRNtkIKKGsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRK--ASYAKRHAVGPVVVHCSA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  219 GIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd17668 155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 37-274 2.95e-47

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 162.59  E-value: 2.95e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   37 AKFPENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14627  48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  113 NRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASF 192
Cdd:cd14627 128 TKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGF 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  193 LNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14627 205 IDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAA 284


                ..
gi 6679553  273 IE 274
Cdd:cd14627 285 LE 286
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 68-269 3.74e-47

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: 159.69  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKLLS 147
Cdd:cd14551   1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGE--TRTISHFHYTTWPDFGVPESPASFLNFLFKVResGCLTPDHGPAVIHCSAGIGRSGT 225
Cdd:cd14551  80 VLVDYTTRKFCIQKVNRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK--SANPPRAGPIVVHCSAGVGRTGT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6679553  226 FSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14551 158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 40-269 1.65e-46

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: 159.23  E-value: 1.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   40 PENRNRNRYRDVSPYDHSRVKL-----QSTENDYINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLN 113
Cdd:cd14612  13 PGHASKDRYKTILPNPQSRVCLrragsQEEEGSYINANYIrGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  114 RTVEKESvKCAQYWPTddREMVFKETGFSVKLLSEdvKSYYTVHLL--QLEnintGETRTISHFHYTTWPDFGVPESPAS 191
Cdd:cd14612  93 KLKEKKE-KCVHYWPE--KEGTYGRFEIRVQDMKE--CDGYTIRDLtiQLE----EESRSVKHYWFSSWPDHQTPESAGP 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679553  192 FLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDT-CLVLMEKGeDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14612 164 LLRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTG-KVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 68-274 2.15e-46

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: 157.77  E-value: 2.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREmVFKEtgFSVKLLS 147
Cdd:cd14555   1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTE-VYGD--IKVTLVE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGclTPDHGPAVIHCSAGIGRSGTFS 227
Cdd:cd14555  77 TEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASN--PPSAGPIVVHCSAGAGRTGCYI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6679553  228 LVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14555 155 VIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 40-267 4.63e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 160.17  E-value: 4.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    40 PENRNRNRYRDVSPYDHSRVKLQS---TENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRT- 115
Cdd:PHA02747  49 PENQPKNRYWDIPCWDHNRVILDSgggSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTk 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   116 -VEKESvKCAQYW-PTDDREMVFKetGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFL 193
Cdd:PHA02747 129 gTNGEE-KCYQYWcLNEDGNIDME--DFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   194 NFLFKV----RESGCLTPDH----GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQL 265
Cdd:PHA02747 206 KFIKIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285


                 ..
gi 6679553   266 RF 267
Cdd:PHA02747 286 LF 287
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 58-275 8.94e-46

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: 156.33  E-value: 8.94e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   58 RVKLQSTEND----YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDRE 133
Cdd:cd14631   1 RVILQPVEDDpssdYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  134 MV--FKETGFSVKLLSEdvksyYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGclTPDHGP 211
Cdd:cd14631  80 VYgdFKVTCVEMEPLAE-----YVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN--PPSAGP 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679553  212 AVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEG 275
Cdd:cd14631 153 IVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA 216
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 37-274 1.16e-45

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: 158.35  E-value: 1.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   37 AKFPENRNRNRYRDVSPYDHSRVKLQSTE----NDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 112
Cdd:cd14629  48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRgvegSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  113 NRTVEKESVKCAQYWPTddrEMVFKETGFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASF 192
Cdd:cd14629 128 TKLREMGREKCHQYWPA---ERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGF 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  193 LNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14629 205 IDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAA 284


                ..
gi 6679553  273 IE 274
Cdd:cd14629 285 LE 286
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 40-277 3.99e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 157.88  E-value: 3.99e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    40 PENRNRNRYRDVSPYDHSRVKLQSTEN-----------------------DYINASLVDIEEAQRSYILTQGPLPNTCCH 96
Cdd:PHA02746  49 KENLKKNRFHDIPCWDHSRVVINAHESlkmfdvgdsdgkkievtsednaeNYIHANFVDGFKEANKFICAQGPKEDTSED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    97 FWLMVWQQKTKAVVMLNRTvEKESVKCAQYWPT-DDREMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHF 175
Cdd:PHA02746 129 FFKLISEHESQVIVSLTDI-DDDDEKCFELWTKeEDSELAFGR--FVAKILDIIEELSFTKTRLMITDKISDTSREIHHF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   176 HYTTWPDFGVPESPASFLNFLFKVRE--------SGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQL 247
Cdd:PHA02746 206 WFPDWPDNGIPTGMAEFLELINKVNEeqaelikqADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                        250       260       270
                 ....*....|....*....|....*....|....
gi 6679553   248 LLNMRKYRMGLIQTPDQLRFSYM----AIIEGAK 277
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKalkyAIIEEAK 319
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 68-269 1.07e-44

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: 152.93  E-value: 1.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDdremvfKET--GFSVKL 145
Cdd:cd14558   1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDE------KKTygDIEVEL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  146 LSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESG----CLTPDHGPAVIHCSAGIG 221
Cdd:cd14558  75 KDTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLpyknSKHGRSVPIVVHCSDGSS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6679553  222 RSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14558 155 RTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 68-269 3.35e-44

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: 151.81  E-value: 3.35e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVFKETGFSVKLLS 147
Cdd:cd14542   1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWP-EEGEEQLQFGPFKISLEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSY-YTVHLLQLENINtgETRTISHFHYTTWPDFGVPESPASFLNFLFKVREsgCLTPDHGPAVIHCSAGIGRSGTF 226
Cdd:cd14542  80 EKRVGPdFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRD--YQGSEDVPICVHCSAGCGRTGTI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6679553  227 SLVDTCLVLMEKG---EDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14542 156 CAIDYVWNLLKTGkipEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 45-267 6.24e-44

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


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 152.71  E-value: 6.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   45 RNRYRDVSPYDHSRVKLQSTEND-----YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNrTVEK 118
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDdplssYINANYIrGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMIT-NIEE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  119 ESVKCAQYWPtdDREMVFKETGFSVK--LLSEDvksyYTVHLLQLENinTGETRTISHFHYTTWPDFGVPESPASFLNFL 196
Cdd:cd14613 107 MNEKCTEYWP--EEQVTYEGIEITVKqvIHADD----YRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679553  197 FKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14613 179 QEVEEArQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 68-272 7.91e-44

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: 150.88  E-value: 7.91e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDremVFKETGFSVKLLS 147
Cdd:cd14552   1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDG---SVSSGDITVELKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHgPAVIHCSAGIGRSGTFS 227
Cdd:cd14552  78 QTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH-PITVHCSAGAGRTGTFC 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6679553  228 LVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14552 157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PHA02738 PHA02738
hypothetical protein; Provisional
 42-272 1.58e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 153.54  E-value: 1.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    42 NRNRNRYRDVSPYDHSRVKLQSTEN--DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKE 119
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPAERNrgDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   120 SVKCAQYWP----TDDREMVFKETGFSVKLLSEDVKSyyTVHLLQleniNTGETRTISHFHYTTWPDFGVPESPASFLNF 195
Cdd:PHA02738 129 REKCFPYWSdveqGSIRFGKFKITTTQVETHPHYVKS--TLLLTD----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNF 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   196 LFKVRES-----------GCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQ 264
Cdd:PHA02738 203 VLEVRQCqkelaqeslqiGHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282


                 ....*...
gi 6679553   265 LRFSYMAI 272
Cdd:PHA02738 283 YFFCYRAV 290
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 68-275 3.78e-43

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: 149.05  E-value: 3.78e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPtDDREMVfkeTGFSVKLLS 147
Cdd:cd14632   1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTY---GDIKITLLK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESgcLTPDHGPAVIHCSAGIGRSGTFS 227
Cdd:cd14632  77 TETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKAS--TPPDAGPVVVHCSAGAGRTGCYI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6679553  228 LVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIEG 275
Cdd:cd14632 155 VLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEA 202
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 45-267 4.87e-42

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: 146.99  E-value: 4.87e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   45 RNRYRDVSPYDHSRVKLQSTEND-----YINASLV-DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEK 118
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIrGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  119 ESvKCAQYWPtDDREMVFKetgfsVKLLSEDVKS--YYTVHLLQLENinTGETRTISHFHYTTWPDFGVPESPASFLNFL 196
Cdd:cd14611  82 NE-KCVLYWP-EKRGIYGK-----VEVLVNSVKEcdNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLM 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679553  197 FKVRESGCLTPDHGPAVIHCSAGIGRSGTF-SLVDTCLVLMEKGEdVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14611 153 LDVEEDRLASPGRGPVVVHCSAGIGRTGCFiATTIGCQQLKEEGV-VDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 47-274 9.67e-42

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: 146.34  E-value: 9.67e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   47 RYRDVSPYDHSRVKL---QSTEN-DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVK 122
Cdd:cd14623   1 RVLQIIPYEFNRVIIpvkRGEENtDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  123 CAQYWPTDDrEMVFKEtgFSVKLLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRES 202
Cdd:cd14623  81 CAQYWPSDG-SVSYGD--ITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679553  203 GCLTPDHgPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14623 158 QQQSGNH-PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 68-269 1.15e-40

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 142.60  E-value: 1.15e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLV--DIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKES-VKCAQYWPTDDRE-MVFKETGFSV 143
Cdd:cd17658   1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENEsREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  144 KLLSEDVKSyYTVHLLQLENINTGET-RTISHFHYTTWPDFGVPESPASFLNFLfkvRESGCLTPDHGPAVIHCSAGIGR 222
Cdd:cd17658  81 KKLKHSQHS-ITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPSAGPIVVHCSAGIGR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6679553  223 SGTFSLVDTCLVLMEKG--EDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd17658 157 TGAYCTIHNTIRRILEGdmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 68-264 2.62e-40

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: 141.50  E-value: 2.62e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDREM-VFKEtgFSVKLL 146
Cdd:cd14557   1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSrAFGD--VVVKIN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENINTGET-RTISHFHYTTWPDFGVPESPasflNFLFKVRE-----SGCLTpdhGPAVIHCSAGI 220
Cdd:cd14557  79 EEKICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDP----HLLLKLRRrvnafNNFFS---GPIVVHCSAGV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6679553  221 GRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQ 264
Cdd:cd14557 152 GRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQ 195
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
40-265 1.64e-38

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 139.46  E-value: 1.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   40 PENRNRNRYRDVSPYDHSRVklqsTEND-YINASLVDIEEAQRsYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVE- 117
Cdd:COG5599  40 INGSPLNRFRDIQPYKETAL----RANLgYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEi 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  118 -KESVKCAQYWPTDDREMVFKetgFSVKLL-SEDVKSYYTVHLLQLENINTG-ETRTISHFHYTTWPDFGVPESPAsFLN 194
Cdd:COG5599 115 sKPKVKMPVYFRQDGEYGKYE---VSSELTeSIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAEA-LKN 190

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679553  195 FLFKVRES-GCLTPDHGPAVIHCSAGIGRSGTFSLvdtCLVLM-----EKGEDVNVKQLLLNMRKYR-MGLIQTPDQL 265
Cdd:COG5599 191 LADLIDKKeKIKDPDKLLPVVHCRAGVGRTGTLIA---CLALSksinaLVQITLSVEEIVIDMRTSRnGGMVQTSEQL 265
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 171-274 1.82e-38

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: 133.64  E-value: 1.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     171 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED-VNVKQLLL 249
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 6679553     250 NMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
171-274 1.82e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 133.64  E-value: 1.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553     171 TISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGED-VNVKQLLL 249
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 6679553     250 NMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 68-274 6.96e-38

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: 135.87  E-value: 6.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINAS--LVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWP-TDDREMVFKETGFSVK 144
Cdd:cd14598   1 YINAShiKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  145 LLSEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFK---VRESGCLTPD----HGPAVIHCS 217
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEiqsVRRHTNSTIDpkspNPPVLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679553  218 AGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 67-272 2.16e-36

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: 131.28  E-value: 2.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   67 DYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQYWPTDDrEMVFKEtgFSVKLL 146
Cdd:cd14622   1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGE--ITIEIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENINTGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGCLTPDHgPAVIHCSAGIGRSGTF 226
Cdd:cd14622  78 NDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH-PIVVHCSAGAGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 6679553  227 SLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAI 272
Cdd:cd14622 157 IALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 68-269 6.77e-35

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: 127.14  E-value: 6.77e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNrTVEKESVKCAQYWPTDDRemvfKETG-FSVKLL 146
Cdd:cd14556   1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLN-QLDPKDQSCPQYWPDEGS----GTYGpIQVEFV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENINTGE--TRTISHFHYTTWPDFG-VPESPASFLNFLFKV----RESGcltpdHGPAVIHCSAG 219
Cdd:cd14556  76 STTIDEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVekwqEQSG-----EGPIVVHCLNG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6679553  220 IGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:cd14556 151 VGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 68-269 4.26e-29

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 111.64  E-value: 4.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKEsvKCAQYWPTDDREMVFKetGFSVKLLS 147
Cdd:cd14550   1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECE--TFKVTLSG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSY-----YTVHLLQLENINTGETRTISHFHYTTWPDfgvPESPAS-FLNFLFKVRESgCLTPDhGPAVIHCSAGIG 221
Cdd:cd14550  77 EDHSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCSPIHtVFELINTVQEW-AQQRD-GPIVVHDRYGGV 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6679553  222 RSGTFSLVDTCLVLMEKGEDVNVKQL--LLNMRkyRMGLIQTPDQLRFSY 269
Cdd:cd14550 152 QAATFCALTTLHQQLEHESSVDVYQVakLYHLM--RPGVFTSKEDYQFLY 199
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 42-272 2.39e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 106.97  E-value: 2.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553    42 NRNRNRYRD------VSPYDHSRVKLQSTENdYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRT 115
Cdd:PHA02740  47 AQAENKAKDenlalhITRLLHRRIKLFNDEK-VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   116 VEKESVKcaQYWPTDDReMVFKETGFSVKLLSEDVKSYYTVHLLQLENiNTGETRTISHFHYTTWPDFGVPESPASFLNF 195
Cdd:PHA02740 126 ADKKCFN--QFWSLKEG-CVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFSHDPDAFIDF 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   196 LFKVRESGCLTPDH------GPAVIHCSAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSY 269
Cdd:PHA02740 202 FCNIDDLCADLEKHkadgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCY 281


                 ...
gi 6679553   270 MAI 272
Cdd:PHA02740 282 HLI 284
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 68-274 1.60e-24

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 99.71  E-value: 1.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNrtvEKESVK-CAQYWPTddremvfKETG----FS 142
Cdd:cd14634   1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPE-------KTSCcygpIQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  143 VKLLSEDVKSYYTVHLLQLENINTGET--RTISHFHYTTWPDF-GVPESPASFLNF---LFKVRESgcLTPDHGPAVIHC 216
Cdd:cd14634  71 VEFVSADIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVvrrLEKWQEQ--YDGREGRTVVHC 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679553  217 SAGIGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14634 149 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 68-274 4.43e-24

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


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 98.44  E-value: 4.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESV-KCAQYWPTDDREmvfKETGFSVKLL 146
Cdd:cd14637   1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQ---QYGPMEVEFV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  147 SEDVKSYYTVHLLQLENIN--TGETRTISHFHYTTWPDF-GVPESPASFLNFLFKV----RESGcltpdHGPAVIHCSAG 219
Cdd:cd14637  78 SGSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVekwqRESG-----EGRTVVHCLNG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6679553  220 IGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14637 153 GGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 68-274 8.09e-22

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 92.40  E-value: 8.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESvkCAQYWPtddREMVFKETGFSVKLLS 147
Cdd:cd14636   1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG--CPQYWP---EEGMLRYGPIQVECMS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGET--RTISHFHYTTWPDF-GVPESPASFLNFLFKVR--ESGCLTPDhGPAVIHCSAGIGR 222
Cdd:cd14636  76 CSMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEkwQEECDEGE-GRTIIHCLNGGGR 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679553  223 SGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14636 155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 68-274 8.92e-22

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 92.06  E-value: 8.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTveKESVKCAQYWPTDDremVFKETGFSVKLLS 147
Cdd:cd14635   1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENG---VHRHGPIQVEFVS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  148 EDVKSYYTVHLLQLENINTGET--RTISHFHYTTWPDF-GVPESPASFLNFLFKV-RESGCLTPDHGPAVIHCSAGIGRS 223
Cdd:cd14635  76 ADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdKWQEEYNGGEGRTVVHCLNGGGRS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 6679553  224 GTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAIIE 274
Cdd:cd14635 156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 68-273 2.49e-21

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 90.89  E-value: 2.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML--NRTV-EKESVkcaqYWPTddREMVFKETGFSVK 144
Cdd:cd17670   1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQGLaEDEFV----YWPS--REESMNCEAFTVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  145 LLSEDV-----KSYYTVHLLQLENINTGETRTISHFHYTTWPDfgvPESPASFLNFLFKVRESGCLTPDhGPAVIHCSAG 219
Cdd:cd17670  75 LISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEFG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679553  220 IGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd17670 151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 68-273 9.34e-20

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: 86.59  E-value: 9.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   68 YINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML---NRTVEKESVkcaqYWPTDDREMVFKetGFSVK 144
Cdd:cd17669   1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLpdgQNMAEDEFV----YWPNKDEPINCE--TFKVT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  145 LLSEDVK--SYYTVHLLQ---LENINTGETRTISHFHYTTWPDfgvPESPASFLNFLFKVRESGCLTPDhGPAVIHCSAG 219
Cdd:cd17669  75 LIAEEHKclSNEEKLIIQdfiLEATQDDYVLEVRHFQCPKWPN---PDSPISKTFELISIIKEEAANRD-GPMIVHDEHG 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679553  220 IGRSGTFSLVDTCLVLMEKGEDVNVKQLLLNMRKYRMGLIQTPDQLRFSYMAII 273
Cdd:cd17669 151 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 46-265 1.25e-10

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 60.88  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553   46 NRYRDVSpydhSRVKLQSTENdyINASLVDIEEaQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRTVEKESVKCAQ 125
Cdd:cd14559   1 NRFTNIQ----TRVSTPVGKN--LNANRVQIGN-KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  126 YWPTDdremvfkETGFSVKLLSEDVKSYY-----TVHLLQLENINTGETRTISHFHYTTWPDFG-------------VPE 187
Cdd:cd14559  74 YFRQS-------GTYGSVTVKSKKTGKDElvdglKADMYNLKITDGNKTITIPVVHVTNWPDHTaisseglkeladlVNK 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679553  188 SPASFLNFLFKVRESGCLTPDHGPAVIHCSAGIGRSGTFSlvdTCLVLMEKGEDVNVKQLLLNMRKYRMG-LIQTPDQL 265
Cdd:cd14559 147 SAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
145-267 1.47e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 58.83  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  145 LLSEDVKSYYTVHLLQLENINTGETRTISHFHYTtWPDFGVPEsPASFLNFLFKVREsgcLTPDHGPAVIHCSAGIGRSG 224
Cdd:COG2453  21 LKREGIDAVVSLTEEEELLLGLLEEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDE---ALREGKKVLVHCRGGIGRTG 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6679553  225 TFslvdTCLVLMEKGedVNVKQLLLNMRKYRMGLIQTPDQLRF 267
Cdd:COG2453  96 TV----AAAYLVLLG--LSAEEALARVRAARPGAVETPAQRAF 132
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 181-267 5.02e-09

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 54.96  E-value: 5.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  181 PDFGVPESPASFLNFLFKVREsgCLTpDHGPAVIHCSAGIGRSGtfsLVDTCLvLMEKGEDVNVKQLLLNMRKYRMGLIQ 260
Cdd:cd14505  81 PDGGVPSDIAQWQELLEELLS--ALE-NGKKVLIHCKGGLGRTG---LIAACL-LLELGDTLDPEQAIAAVRALRPGAIQ 153


                ....*..
gi 6679553  261 TPDQLRF 267
Cdd:cd14505 154 TPKQENF 160
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 189-267 2.44e-05

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 43.11  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  189 PASFLNFLFKVREsgCLTPDHgPAVIHCSAGIGRSGTFslvdTCLVLMEKGeDVNVKQLLLNMRKYR-MGLIQTPDQLRF 267
Cdd:cd14494  39 LAMVDRFLEVLDQ--AEKPGE-PVLVHCKAGVGRTGTL----VACYLVLLG-GMSAEEAVRIVRLIRpGGIPQTIEQLDF 110
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 209-255 6.09e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 40.05  E-value: 6.09e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6679553  209 HGPAVIHCSAGIGRSGTFSLVdtCLVLMEKGEDVNVKQLLLNMRKYR 255
Cdd:cd14529  89 PGPVLIHCKHGKDRTGLVSAL--YRIVYGGSKEEANEDYRLSNRHLE 133
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 181-267 6.97e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 39.57  E-value: 6.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  181 PDFGVP--ESPASFLNFLFKVRESGcltpdhGPAVIHCSAGIGRSGTFSlvdTC-LVLMEK--GEDVnVKQLllnmRKYR 255
Cdd:cd14504  58 EDYTPPtlEQIDEFLDIVEEANAKN------EAVLVHCLAGKGRTGTML---ACyLVKTGKisAVDA-INEI----RRIR 123

                        90
                ....*....|..
gi 6679553  256 MGLIQTPDQLRF 267
Cdd:cd14504 124 PGSIETSEQEKF 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 172-267 8.40e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 40.41  E-value: 8.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679553  172 ISHFHYTtWPDFGVPeSPASFLN----FLFKVRESGcltpdhgPAVIHCSAGIGRSGtfsLVDTCLVLMekGEDVNVKQL 247
Cdd:cd14506  77 IYFYNFG-WKDYGVP-SLTTILDivkvMAFALQEGG-------KVAVHCHAGLGRTG---VLIACYLVY--ALRMSADQA 142

                        90       100
                ....*....|....*....|
gi 6679553  248 LLNMRKYRMGLIQTPDQLRF 267
Cdd:cd14506 143 IRLVRSKRPNSIQTRGQVLC 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 212-269 1.82e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 38.72  E-value: 1.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679553  212 AVIHCSAGIGRSGTFslvdTCLVLMEKG--EDVNVKQLLLNMRKYRMGL--IQTPDQLRFSY 269
Cdd:cd14497  98 AVVHCKAGKGRTGTV----ICAYLLYYGqySTADEALEYFAKKRFKEGLpgVTIPSQLRYLQ 155
 
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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