NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|333470564|gb|EAA01059|]
View 

AGAP001109-PA [Anopheles gambiae str. PEST]

Protein Classification

CRAL-TRIO domain-containing protein( domain architecture ID 13641064)

CRAL-TRIO domain-containing protein act as a lipid binding protein which may bind small lipophilic molecules such as retinal, inositol, and vitamin E; similar to fungal phosphatidylinositol transfer protein SFH5, a non-classical phosphatidylinositol (PtdIns) transfer protein (PITP) which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 411-681 3.90e-180

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: 513.45  E-value: 3.90e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 411 GKMGLIREYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGP 490
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 491 LPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVR 570
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 571 CVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 650
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333470564 651 GTADIKGTVEKIRSQRAYSIQMPDQYVFCHL 681
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-226 3.98e-31

CRAL/TRIO domain;


:

Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.90  E-value: 3.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   83 GKFTILPGRDASGAAIALFTANLHYPMTVTHKTTLQGVVYQLDVALQSS-ETQKAGLVFIYDMSTSKYSNFD---YDLSQ 158
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDwwsISLLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564  159 KILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVF---TVSIPQLSLHVPRESLPVRLGG 226
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVflkNSNEEELEKYIPPEQLPKEYGG 151
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 411-681 3.90e-180

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: 513.45  E-value: 3.90e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 411 GKMGLIREYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGP 490
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 491 LPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVR 570
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 571 CVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 650
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333470564 651 GTADIKGTVEKIRSQRAYSIQMPDQYVFCHL 681
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
414-685 1.57e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 350.42  E-value: 1.57e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   414 GLIREYTEIKARAP-DGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPaTDYINANFVDGYKQKNAYISTQGPLP 492
Cdd:smart00194   1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   493 KTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCV 572
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   573 SHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT 652
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQS-------------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                          250       260       270
                   ....*....|....*....|....*....|...
gi 333470564   653 ADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
439-685 3.37e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 346.15  E-value: 3.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  439 NLAKNRYTDVLCYDHSRVVLSQEEDDpaTDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  519 RGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNE-DYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQ 597
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  598 RAREKQaemvralgdlwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYV 677
Cdd:pfam00102 159 KVRKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 333470564  678 FCHLALIE 685
Cdd:pfam00102 227 FLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 417-686 1.36e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 251.38  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 417 REYTEIKARAPDGTFTHAKLRNNLakNRYTDVLCYDHSRVVLSQEEDdpATDYINANFVDGYKQKNAYISTQGPLPKTSY 496
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 497 DFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNiKTDEVRCVSHWQ 576
Cdd:PHA02738 105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 577 FTSWPDYGVPSSAKAMLNFLQRAREKQAEMvrALGDLWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD 654
Cdd:PHA02738 184 FTAWPDHDVPKNTSEFLNFVLEVRQCQKEL--AQESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVS 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 333470564 655 IKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:PHA02738 262 IPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
432-690 6.43e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 125.59  E-value: 6.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 432 THAKLRNNLAKNRYTDVLCYDHSRVvlsqEEDDPatdYINANFVDGyKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIV 511
Cdd:COG5599   35 QYLQNINGSPLNRFRDIQPYKETAL----RANLG---YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 512 MTTRVME--RGRAKCGQYWEPTEgglaEYGSFRLRTMSIET---NEDYTVVELEIRNIKTD-EVRCVSHWQFTSWPDYGV 585
Cdd:COG5599  107 VLASDDEisKPKVKMPVYFRQDG----EYGKYEVSSELTESiqlRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 586 PsSAKAMLNFLQRAREKQAEmvralgdlwAGHPRGPPiVVHCSAGIGRTGTFItLDICISRL---EDVGTADIKGTVEKI 662
Cdd:COG5599  183 I-SAEALKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSinaLVQITLSVEEIVIDM 250

                        250       260
                 ....*....|....*....|....*....
gi 333470564 663 RSQRAYSI-QMPDQYVFchlaLIEYALSR 690
Cdd:COG5599  251 RTSRNGGMvQTSEQLDV----LVKLAEQQ 275
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-226 3.98e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.90  E-value: 3.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   83 GKFTILPGRDASGAAIALFTANLHYPMTVTHKTTLQGVVYQLDVALQSS-ETQKAGLVFIYDMSTSKYSNFD---YDLSQ 158
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDwwsISLLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564  159 KILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVF---TVSIPQLSLHVPRESLPVRLGG 226
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVflkNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 81-227 1.74e-28

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 111.66  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  81 ETGKFTILPGRDASGAAIALFTANLHYPMTVTHKTTLQGVVYQLDVALQSSETQKAGLVFIYDMSTSKYSNF-DYDLSQK 159
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 160 ILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS--IPQLSLHVPRESLPVRLGGT 227
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 79-229 7.84e-28

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 109.70  E-value: 7.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564    79 ELETGKFTILPGR--DASGAAIALFTANLHYPMTVTHKTTLQGVVYQLD--VALQSSETQKAGLVFIYDMSTSKYSNFDY 154
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564   155 DLSQKILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS---IPQLSLHVPRESLPVRLGGTLE 229
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 411-681 3.90e-180

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: 513.45  E-value: 3.90e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 411 GKMGLIREYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGP 490
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 491 LPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVR 570
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 571 CVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 650
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333470564 651 GTADIKGTVEKIRSQRAYSIQMPDQYVFCHL 681
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
414-685 1.57e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 350.42  E-value: 1.57e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   414 GLIREYTEIKARAP-DGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPaTDYINANFVDGYKQKNAYISTQGPLP 492
Cdd:smart00194   1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   493 KTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCV 572
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   573 SHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT 652
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQS-------------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKE 226

                          250       260       270
                   ....*....|....*....|....*....|...
gi 333470564   653 ADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:smart00194 227 VDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
439-685 3.37e-115

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 346.15  E-value: 3.37e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  439 NLAKNRYTDVLCYDHSRVVLSQEEDDpaTDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  519 RGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNE-DYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQ 597
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  598 RAREKQaemvralgdlwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYV 677
Cdd:pfam00102 159 KVRKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYI 226


                  ....*...
gi 333470564  678 FCHLALIE 685
Cdd:pfam00102 227 FLYDAILE 234
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 439-685 4.85e-90

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: 281.21  E-value: 4.85e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 519 RGRAKCGQYWePTEGGlAEYGSFR---LRTMSIETnedYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNF 595
Cdd:cd14553   83 RSRVKCDQYW-PTRGT-ETYGLIQvtlLDTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 596 LQRarekqaemVRALGDLWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQ 675
Cdd:cd14553  158 LRR--------VKACNPPDAG-----PIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQ 224

                        250
                 ....*....|
gi 333470564 676 YVFCHLALIE 685
Cdd:cd14553  225 YIFIHDALLE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 469-680 1.37e-88

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: 275.70  E-value: 1.37e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSI 548
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCS 628
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR-------------KPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333470564 629 AGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 444-680 3.99e-81

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: 257.28  E-value: 3.99e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 444 RYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAK 523
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 524 CGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIktDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQrarekq 603
Cdd:cd14548   81 CDHYW-PFDQDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVR------ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333470564 604 aeMVRAlgdlWAGHPRGPPIvVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14548  152 --LVRD----YIKQEKGPTI-VHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PHA02738 PHA02738
hypothetical protein; Provisional
 417-686 1.36e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 251.38  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 417 REYTEIKARAPDGTFTHAKLRNNLakNRYTDVLCYDHSRVVLSQEEDdpATDYINANFVDGYKQKNAYISTQGPLPKTSY 496
Cdd:PHA02738  29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERN--RGDYINANYVDGFEYKKKFICGQAPTRQTCY 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 497 DFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNiKTDEVRCVSHWQ 576
Cdd:PHA02738 105 DFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 577 FTSWPDYGVPSSAKAMLNFLQRAREKQAEMvrALGDLWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD 654
Cdd:PHA02738 184 FTAWPDHDVPKNTSEFLNFVLEVRQCQKEL--AQESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVS 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 333470564 655 IKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:PHA02738 262 IPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 417-687 6.51e-77

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: 248.03  E-value: 6.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 417 REYTEIKaraPDGTFT--HAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKT 494
Cdd:cd14626   20 QEYESID---PGQQFTweNSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPET 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 495 SYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSH 574
Cdd:cd14626   97 LSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW-PIRGT-ETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 575 WQFTSWPDYGVPSSAKAMLNFLQRarekqaemVRALGDLWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD 654
Cdd:cd14626  175 FQFMAWPDHGVPEYPTPILAFLRR--------VKACNPPDAG-----PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVD 241

                        250       260       270
                 ....*....|....*....|....*....|...
gi 333470564 655 IKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 687
Cdd:cd14626  242 IYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 469-680 7.21e-76

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: 242.64  E-value: 7.21e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLaEYGSFRLRTMSI 548
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW-PKEGTE-TYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIK------TDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRARekqaemvralgdlwAGHPRGP- 621
Cdd:cd14549   79 EVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSS--------------AANPPGAg 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 622 PIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14549  145 PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 439-686 2.08e-74

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: 240.44  E-value: 2.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEEDDPA-TDYINANFV-------DGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLI 510
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 511 VMTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIK-TDEVRCVSHWQFTSWPDYGVPSSA 589
Cdd:cd14544   81 VMTTKEVERGKNKCVRYW-PDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 590 KAMLNFLQRAREKQAEMvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTA---DIKGTVEKIRSQR 666
Cdd:cd14544  160 GGVLNFLEDVNQRQESL-----------PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQR 228

                        250       260
                 ....*....|....*....|
gi 333470564 667 AYSIQMPDQYVFCHLALIEY 686
Cdd:cd14544  229 SGMVQTEAQYKFIYVAVAQY 248
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 443-678 5.23e-74

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: 238.56  E-value: 5.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEeDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQ-SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWePTEGGLaEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREK 602
Cdd:cd14615   80 KCEEYW-PSKQKK-DYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333470564 603 QAEmvralgdlwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14615  158 MKQ-----------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 442-681 5.75e-74

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: 238.83  E-value: 5.75e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 442 KNRYTDVLCYDHSRVVLSQEEDDpaTDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGR 521
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 522 AKCGQYW--EPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRA 599
Cdd:cd14545   79 IKCAQYWpqGEGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 600 REKqaemvralGDLWAGHprGPPiVVHCSAGIGRTGTFITLDICISRLE--DVGTADIKGTVEKIRSQRAYSIQMPDQYV 677
Cdd:cd14545  159 RES--------GSLSSDV--GPP-VVHCSAGIGRSGTFCLVDTCLVLIEkgNPSSVDVKKVLLEMRKYRMGLIQTPDQLR 227


                 ....
gi 333470564 678 FCHL 681
Cdd:cd14545  228 FSYL 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 418-688 3.87e-73

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: 238.01  E-value: 3.87e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 418 EYTEIKARAPDGTFT--HAKLRNNLAKNRYTDVLCYDHSRVVLS--QEEDDPATDYINANFVDGYKQKNAYISTQGPLPK 493
Cdd:cd17667    4 DFEEVQRCTADMNITaeHSNHPDNKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 494 TSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEV---- 569
Cdd:cd17667   84 TFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYW-PTENS-EEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGqkgn 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 570 -------RCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDI 642
Cdd:cd17667  162 pkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAART-------------PEMGPVLVHCSAGVGRTGTYIVIDS 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 333470564 643 CISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAL 688
Cdd:cd17667  229 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 434-682 9.20e-73

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: 235.88  E-value: 9.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 434 AKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMT 513
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 514 TRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAML 593
Cdd:cd14554   81 TKLREMGREKCHQYW-PAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 594 NFL---QRAREKQAEmvralgdlwaghprGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSI 670
Cdd:cd14554  159 DFIgqvHKTKEQFGQ--------------EGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMV 224

                        250
                 ....*....|..
gi 333470564 671 QMPDQYVFCHLA 682
Cdd:cd14554  225 QTEDQYQFCYRA 236
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 443-680 5.90e-72

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: 233.06  E-value: 5.90e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKN-AYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERgR 521
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 522 AKCGQYWePTEGGLaEYGSFRLRTMSIETNEDYTVVELEIRNikTDEVRCVSHWQFTSWPDYGVPSSAKAMLnflqrare 601
Cdd:cd14547   80 EKCAQYW-PEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLL-------- 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 602 kqaEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14547  148 ---SLVQEVEEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 405-685 1.05e-70

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: 231.91  E-value: 1.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 405 QMVRERGKMGLIREYTEIKaraPDGTFT--HAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKN 482
Cdd:cd14625   14 ERLKANDNLKLSQEYESID---PGQQFTweHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 483 AYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEgGLAEYGSFRLRTMSIETNEDYTVVELEIR 562
Cdd:cd14625   91 AYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW-PSR-GTETYGMIQVTLLDTIELATFCVRTFSLH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 563 NIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREkqaemvralgdlwAGHPRGPPIVVHCSAGIGRTGTFITLDI 642
Cdd:cd14625  169 KNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-------------CNPPDAGPIVVHCSAGVGRTGCFIVIDA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 333470564 643 CISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14625  236 MLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 404-685 1.45e-70

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: 231.54  E-value: 1.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 404 VQMVRERGKMGLIREYTEIKaraPDGTFT--HAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQK 481
Cdd:cd14624   13 IERLKANDNLKFSQEYESID---PGQQFTweHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 482 NAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEgGLAEYGSFRLRTMSIETNEDYTVVELEI 561
Cdd:cd14624   90 NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYW-PSR-GTETYGLIQVTLLDTVELATYCVRTFAL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 562 RNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREkqaemvralgdlwAGHPRGPPIVVHCSAGIGRTGTFITLD 641
Cdd:cd14624  168 YKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-------------CNPPDAGPMVVHCSAGVGRTGCFIVID 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 333470564 642 ICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14624  235 AMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 419-687 4.44e-70

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: 230.30  E-value: 4.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 419 YTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDpatdYINANFVDGYKQKNAYISTQGPLPKTSYDF 498
Cdd:cd14608    5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND----YINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 499 WRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLA--EYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQ 576
Cdd:cd14608   81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 577 FTSWPDYGVPSSAKAMLNFLQRAREKqaemvralGDLwagHPRGPPIVVHCSAGIGRTGTFITLDICI---SRLEDVGTA 653
Cdd:cd14608  161 YTTWPDFGVPESPASFLNFLFKVRES--------GSL---SPEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSV 229

                        250       260       270
                 ....*....|....*....|....*....|....
gi 333470564 654 DIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 687
Cdd:cd14608  230 DIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGA 263
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 418-690 5.25e-69

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 228.76  E-value: 5.25e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 418 EYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEE-------------------DDPATDYINANFVDGY 478
Cdd:PHA02746  30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHEslkmfdvgdsdgkkievtsEDNAENYIHANFVDGF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 479 KQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVmERGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVE 558
Cdd:PHA02746 110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTR 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 559 LEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVRALGDlwagHPRGP-PIVVHCSAGIGRTGTF 637
Cdd:PHA02746 189 LMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADN----DPQTLgPIVVHCSAGIGRAGTF 264

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 333470564 638 ITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALiEYALSR 690
Cdd:PHA02746 265 CAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL-KYAIIE 316
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 443-680 8.00e-69

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: 225.15  E-value: 8.00e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFlqrarek 602
Cdd:cd14619   81 KCEHYW-PLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF------- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564 603 qAEMVRALGDLwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14619  153 -RRLLRQWLDQ---TMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 468-678 3.59e-68

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: 222.59  E-value: 3.59e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 468 DYINANFVD----GYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRL 543
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYW-PDLGETMQFGNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 544 RTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVralgdlwaghprgPPI 623
Cdd:cd14541   80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV-------------EPT 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564 624 VVHCSAGIGRTGTFITLD--IC-ISRLEDVGTADIkgtVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14541  147 VVHCSAGIGRTGVLITMEtaMClIEANEPVYPLDI---VRTMRDQRAMLIQTPSQYRF 201
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 443-681 1.67e-67

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: 221.33  E-value: 1.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRN-IKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFlqrare 601
Cdd:cd14617   81 KCDHYW-PADQDSLYYGDLIVQMLSESVLPEWTIREFKICSeEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQF------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 602 kqaemVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHL 681
Cdd:cd14617  154 -----VRTVRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 443-684 1.88e-67

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: 221.36  E-value: 1.88e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREk 602
Cdd:cd14618   81 LCDHYW-PSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 603 QAEMVRALGdlwaghprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLA 682
Cdd:cd14618  159 HVQATKGKG----------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 ..
gi 333470564 683 LI 684
Cdd:cd14618  229 IL 230
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 445-685 2.32e-67

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: 221.35  E-value: 2.32e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 445 YTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKC 524
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 525 GQYWepTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEV---RCVSHWQFTSWPDYGVPSSAKAMLNFLQRare 601
Cdd:cd14620   81 YQYW--PDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKK--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 602 kqaemVRALGDLWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHL 681
Cdd:cd14620  156 -----VKSVNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225


                 ....
gi 333470564 682 ALIE 685
Cdd:cd14620  226 ALLE 229
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 419-683 5.32e-67

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: 221.38  E-value: 5.32e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 419 YTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDpatdYINANFVDGYKQKNAYISTQGPLPKTSYDF 498
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 499 WRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEG----GLAEYGsFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSH 574
Cdd:cd14607   80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYW-PTDEeevlSFKETG-FSVKLLSEDVKSYYTVHLLQLENINSGETRTISH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 575 WQFTSWPDYGVPSSAKAMLNFLQRAREKqaemvRALGdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLE--DVGT 652
Cdd:cd14607  158 FHYTTWPDFGVPESPASFLNFLFKVRES-----GSLS------PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDS 226

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333470564 653 ADIKGTVEKIRSQRAYSIQMPDQYVFCHLAL 683
Cdd:cd14607  227 VDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 434-680 6.75e-67

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: 220.53  E-value: 6.75e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 434 AKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMT 513
Cdd:cd14614    7 ADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 514 TRVMERGRAKCGQYWEPTEGGLAeYGSFRLRTMSIETNEDYTVVELEIRniKTDEVRCVSHWQFTSWPDYGVPS--SAKA 591
Cdd:cd14614   87 TQCNEKRRVKCDHYWPFTEEPVA-YGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAES 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 592 MLNFLQRAREKqaemvralgdlwAGHPRGpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQ 671
Cdd:cd14614  164 ILQFVQMVRQQ------------AVKSKG-PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230


                 ....*....
gi 333470564 672 MPDQYVFCH 680
Cdd:cd14614  231 TEEQYIFIH 239
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 439-686 1.16e-66

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: 220.27  E-value: 1.16e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQ-EEDDPATDYINANFV--------DGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLL 509
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 510 IVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNI-KTDEVRCVSHWQFTSWPDYGVPSS 588
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYW-PDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 589 AKAMLNFLQRAREKQAEMVRAlgdlwaghprgPPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIKGTVEKIRSQ 665
Cdd:cd14605  161 PGGVLDFLEEVHHKQESIMDA-----------GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQ 229

                        250       260
                 ....*....|....*....|.
gi 333470564 666 RAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14605  230 RSGMVQTEAQYRFIYMAVQHY 250
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 439-687 8.09e-66

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 219.87  E-value: 8.09e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEedDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:PHA02742  52 NMKKCRYPDAPCFDRNRVILKIE--DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 519 RGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQR 598
Cdd:PHA02742 130 DGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 599 AREkqAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:PHA02742 210 VRE--ADLKADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                 ....*....
gi 333470564 679 CHLALIEYA 687
Cdd:PHA02742 288 CYFIVLIFA 296
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 415-678 1.11e-65

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: 1.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 415 LIREYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDdpatdYINANFVD----GYKQKNAYISTQGP 490
Cdd:cd14600   16 VLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNED-----YINASYVNmeipSANIVNKYIATQGP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 491 LPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVR 570
Cdd:cd14600   91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYW-PDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEER 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 571 CVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVralgdlwaghprgpPIVVHCSAGIGRTGTFITLD--IC-ISRL 647
Cdd:cd14600  170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE--------------PVLVHCSAGIGRTGVLVTMEtaMClTERN 235

                        250       260       270
                 ....*....|....*....|....*....|.
gi 333470564 648 EDVGTADIkgtVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14600  236 QPVYPLDI---VRKMRDQRAMMVQTSSQYKF 263
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 439-688 1.03e-64

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: 214.50  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 519 RGRAKCGQYWePTEGGLaeYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQR 598
Cdd:cd14630   83 VGRVKCVRYW-PDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 599 ARekqaemvralgdlWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14630  160 VK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226

                        250
                 ....*....|
gi 333470564 679 CHLALIEYAL 688
Cdd:cd14630  227 VHDAILEACL 236
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 400-686 2.50e-64

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


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 215.37  E-value: 2.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 400 IEQIVQMVRERGKMGLIREYTEI-KARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGY 478
Cdd:cd14627   13 IQKLAQVEVGEHVTGMELEFKRLaNSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 479 KQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVE 558
Cdd:cd14627   93 RQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW-PAERS-ARYQYFVVDPMAEYNMPQYILRE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 559 LEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMvralgdlwaghPRGPPIVVHCSAGIGRTGTFI 638
Cdd:cd14627  171 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF-----------GQDGPISVHCSAGVGRTGVFI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 333470564 639 TLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14627  240 TLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 418-685 7.59e-64

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: 213.15  E-value: 7.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 418 EYTEIKARAP-----DGTFTHA-KLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPL 491
Cdd:cd14603    3 EFSEIRACSAafkadYVCSTVAgGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 492 PKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTM-SIETNEDYTVVELEIRniKTDEVR 570
Cdd:cd14603   83 SHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYW-AQEQEPLQTGPFTITLVkEKRLNEEVILRTLKVT--FQKESR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 571 CVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEmvralgdlwaghprGP-PIVVHCSAGIGRTGTFITLDIcISRL-- 647
Cdd:cd14603  160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGS--------------GPePLCVHCSAGCGRTGVICTVDY-VRQLll 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 333470564 648 -----EDVGTADIkgtVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14603  225 tqripPDFSIFDV---VLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 400-686 1.41e-63

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: 213.44  E-value: 1.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 400 IEQIVQMVRERGKMGLIREYTEI-KARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGY 478
Cdd:cd14628   12 IQKLTQIETGENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 479 KQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVE 558
Cdd:cd14628   92 RQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW-PAERS-ARYQYFVVDPMAEYNMPQYILRE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 559 LEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMvralgdlwaghPRGPPIVVHCSAGIGRTGTFI 638
Cdd:cd14628  170 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF-----------GQDGPISVHCSAGVGRTGVFI 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 333470564 639 TLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14628  239 TLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 469-680 1.59e-63

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: 210.18  E-value: 1.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVD-GYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMS 547
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYW-PSGEYEGEYGDLTVELVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IETNED--YTVVELEIRNiKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQaemvralgdlwAGHPRGPPIVV 625
Cdd:cd18533   80 EEENDDggFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELN-----------DSASLDPPIIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333470564 626 HCSAGIGRTGTFITLDICISRLEDVGTAD---------IKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd18533  148 HCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 469-684 5.62e-63

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: 208.68  E-value: 5.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSI 548
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW-PADGS-EEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDE--------VRCVSHWQFTSWPDYGVPSSAKAMLNFLQRARE-KQAEMvralgdlwaghpr 619
Cdd:cd17668   79 QVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYaKRHAV------------- 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333470564 620 gPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALI 684
Cdd:cd17668  146 -GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 434-688 1.39e-62

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: 211.04  E-value: 1.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 434 AKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMT 513
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 514 TRVMERGRAKCGQYWepTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNI----KTDEVRCVSHWQFTSWPDYGVPSSA 589
Cdd:cd14621  127 TNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 590 KAMLNFLQRarekqaemVRALGDLWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYS 669
Cdd:cd14621  205 IGMLKFLKK--------VKNCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQM 271

                        250
                 ....*....|....*....
gi 333470564 670 IQMPDQYVFCHLALIEYAL 688
Cdd:cd14621  272 VQTDMQYVFIYQALLEHYL 290
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 439-686 2.56e-62

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: 208.97  E-value: 2.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEEDD-PATDYINANFV------DGYKQKNaYISTQGPLPKTSYDFWRMVWEQHCLLIV 511
Cdd:cd14606   18 NKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRVIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 512 MTTRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNI-KTDEVRCVSHWQFTSWPDYGVPSSAK 590
Cdd:cd14606   97 MTTREVEKGRNKCVPYW-PEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLdNGELIREIWHYQYLSWPDHGVPSEPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 591 AMLNFLQRAREKQAEMvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIKGTVEKIRSQRA 667
Cdd:cd14606  176 GVLSFLDQINQRQESL-----------PHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                        250
                 ....*....|....*....
gi 333470564 668 YSIQMPDQYVFCHLALIEY 686
Cdd:cd14606  245 GMVQTEAQYKFIYVAIAQF 263
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 414-678 4.47e-62

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 209.86  E-value: 4.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 414 GLIR-EYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLsQEEDDPATDYINANFVDGYKQKNAYISTQGPLP 492
Cdd:PHA02747  25 GIIRdEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 493 KTSYDFWRMVWEQHCLLIVMTTRVME-RGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRC 571
Cdd:PHA02747 104 ETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRK 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 572 VSHWQFTSWPDYGVPSSAKAMLNFLQ---RAREKQAEMVRALGDLWAghprgpPIVVHCSAGIGRTGTFITLDICISRLE 648
Cdd:PHA02747 184 ISHFQCSEWFEDETPSDHPDFIKFIKiidINRKKSGKLFNPKDALLC------PIVVHCSDGVGKTGIFCAVDICLNQLV 257

                        250       260       270
                 ....*....|....*....|....*....|
gi 333470564 649 DVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:PHA02747 258 KRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 424-686 1.24e-61

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: 208.04  E-value: 1.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 424 ARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVW 503
Cdd:cd14629   38 SKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 504 EQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDY 583
Cdd:cd14629  118 EHNSTIVVMLTKLREMGREKCHQYW-PAERS-ARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQ 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 584 GVPSSAKAMLNFLQRAREKQAEMvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIR 663
Cdd:cd14629  196 GVPKTGEGFIDFIGQVHKTKEQF-----------GQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLR 264

                        250       260
                 ....*....|....*....|...
gi 333470564 664 SQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14629  265 TQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 469-685 1.65e-61

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: 204.53  E-value: 1.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFV--DGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYW-EPTEGGLAEYGSFRLRT 545
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWpDSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 546 MSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQaemvralgdlwaghpRGPPIVV 625
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH---------------NSGPIVV 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 626 HCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14538  146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 455-688 3.41e-61

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: 204.48  E-value: 3.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 455 RVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGG 534
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW-PDDTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 535 LaeYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRARekqaemvralgdlW 614
Cdd:cd14631   80 V--YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------------L 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 333470564 615 AGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAL 688
Cdd:cd14631  145 SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 400-688 9.23e-61

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: 205.28  E-value: 9.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 400 IEQIVQMVRERGkMGLIREYtEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYK 479
Cdd:cd14633    3 LQHITQMKCAEG-YGFKEEY-ESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 480 QKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLaeYGSFRLRTMSIETNEDYTVVEL 559
Cdd:cd14633   81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW-PDDTEI--YKDIKVTLIETELLAEYVIRTF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 560 EIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCSAGIGRTGTFIT 639
Cdd:cd14633  158 AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP-------------PNAGPLVVHCSAGAGRTGCFIV 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 333470564 640 LDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAL 688
Cdd:cd14633  225 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 469-680 4.51e-60

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: 200.82  E-value: 4.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSI 548
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTD-EVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRarekqaemVRALGDLWAGhprgpPIVVHC 627
Cdd:cd14557   81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDPHLLLKLRRR--------VNAFNNFFSG-----PIVVHC 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 333470564 628 SAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 469-683 8.14e-60

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: 200.19  E-value: 8.14e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAeYGSFRLRTMSI 548
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW-PEDGSVS-SGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwagHPRGPPIVVHCS 628
Cdd:cd14552   79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ------------QSGNHPITVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333470564 629 AGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLAL 683
Cdd:cd14552  147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 469-688 1.00e-59

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: 199.76  E-value: 1.00e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYW-EPTEgglaEYGSFRLRTMS 547
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWpDDTE----VYGDIKVTLVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHC 627
Cdd:cd14555   77 TEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP-------------PSAGPIVVHC 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564 628 SAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAL 688
Cdd:cd14555  144 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 441-686 1.81e-59

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: 200.83  E-value: 1.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 441 AKNRYTDVLCYDHSRVVL----SQEEDDpatDYINANFVDGYKQK-NAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTR 515
Cdd:cd14612   17 SKDRYKTILPNPQSRVCLrragSQEEEG---SYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 516 VMERgRAKCGQYWEPTEGglaEYGSFRLRTMSIETNEDYTVVELEIRNikTDEVRCVSHWQFTSWPDYGVPSSAKAMLNF 595
Cdd:cd14612   94 LKEK-KEKCVHYWPEKEG---TYGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAGPLLRL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 596 LQRAREKQaemvralgdLWAGHPrgPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQ 675
Cdd:cd14612  168 VAEVEESR---------QTAASP--GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQ 236

                        250
                 ....*....|.
gi 333470564 676 YVFCHLALIEY 686
Cdd:cd14612  237 YQFLHHTLALY 247
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 469-687 3.47e-59

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: 198.83  E-value: 3.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVD---GYKQKNaYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGG---LAEYGSFR 542
Cdd:cd14540    1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYW-PTLGGehdALTFGEYK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 543 LRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQrarEKQAEMVRALGDLwAGHPRGPP 622
Cdd:cd14540   79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLE---EINSVRRHTNQDV-AGHNRNPP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333470564 623 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 687
Cdd:cd14540  155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 444-685 5.97e-59

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: 198.73  E-value: 5.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 444 RYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAK 523
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 524 CGQYWePTEgGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQ 603
Cdd:cd14623   81 CAQYW-PSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 604 AEMvralgdlwAGHprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLAL 683
Cdd:cd14623  159 QQS--------GNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226


                 ..
gi 333470564 684 IE 685
Cdd:cd14623  227 QE 228
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 427-685 4.85e-58

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: 198.36  E-value: 4.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 427 PDGTFThAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKN-AYISTQGPLPKTSYDFWRMVWEQ 505
Cdd:cd14610   33 PNATNV-AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWES 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 506 HCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIET-NEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYG 584
Cdd:cd14610  112 GCVVIVMLTPLAENGVKQCYHYW-PDEGS-NLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 585 VPSSAKAMLNFlqraREKQAEMVRAlgdlwaghpRGPPIVVHCSAGIGRTGTFITLDICISRL-EDVGTADIKGTVEKIR 663
Cdd:cd14610  190 VPASTRSLLDF----RRKVNKCYRG---------RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLR 256

                        250       260
                 ....*....|....*....|..
gi 333470564 664 SQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14610  257 DQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 443-680 1.32e-57

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: 194.74  E-value: 1.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRniKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREK 602
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564 603 QAEmvralgdlwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14616  159 RAH-------------DNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 442-686 1.67e-57

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: 195.85  E-value: 1.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 442 KNRYTDVLCYDHSRVVL-SQEEDDPATDYINANFVDGY-KQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMER 519
Cdd:cd14613   28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 520 GRaKCGQYWePTEGGLaeYGSFRLRTMSIETNEDYTvveLEIRNIKTD-EVRCVSHWQFTSWPDYGVPSSAKAMLNFLQR 598
Cdd:cd14613  108 NE-KCTEYW-PEEQVT--YEGIEITVKQVIHADDYR---LRLITLKSGgEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 599 ARE--KQAEmvralgdlwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQY 676
Cdd:cd14613  181 VEEarQQAE------------PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQY 248

                        250
                 ....*....|
gi 333470564 677 VFCHLALIEY 686
Cdd:cd14613  249 QFVHHVLSLY 258
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 469-678 1.88e-57

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: 193.59  E-value: 1.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWepTEGGLAEYGSFRLRTMSI 548
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYW--PDQGCWTYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTD----EVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREkqaemvralgdlwAGHPRGPPIV 624
Cdd:cd14551   79 VVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-------------ANPPRAGPIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 333470564 625 VHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14551  146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 469-688 2.37e-57

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: 193.73  E-value: 2.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLaeYGSFRLRTMSI 548
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYW-PDDSDT--YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAemvralgdlwaghPRGPPIVVHCS 628
Cdd:cd14632   78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP-------------PDAGPVVVHCS 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 629 AGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAL 688
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 410-685 3.29e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 196.03  E-value: 3.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 410 RGKMGLIREYTEIKA-RAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINAN-FVDGYKQKNAYIST 487
Cdd:cd14609   12 RNRDRLAKEWQALCAyQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIAT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 488 QGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMSIET-NEDYTVVELEIRNIKT 566
Cdd:cd14609   92 QGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYW-PDEGS-SLYHIYEVNLVSEHIwCEDFLVRSFYLKNVQT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 567 DEVRCVSHWQFTSWPDYGVPSSAKAMLNFlqraREKQAEMVRAlgdlwaghpRGPPIVVHCSAGIGRTGTFITLDICISR 646
Cdd:cd14609  170 QETRTLTQFHFLSWPAEGIPSSTRPLLDF----RRKVNKCYRG---------RSCPIIVHCSDGAGRTGTYILIDMVLNR 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 333470564 647 L-EDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14609  237 MaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 418-686 5.80e-56

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: 192.52  E-value: 5.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 418 EYTEIKARAPDGTFTHAKLRNNLAKNRYTDVLCYDHSRVVLSQEEDDPaTDYINANF----VDGykQKNAYISTQGPLPK 493
Cdd:cd14599   17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHikvtVGG--EEWHYIATQGPLPH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 494 TSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEP--TEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEVRC 571
Cdd:cd14599   94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 572 VSHWQFTSWPDYGVPSSAKAMLNFLQrarEKQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVG 651
Cdd:cd14599  174 VWHLQYTDWPDHGCPEEVQGFLSYLE---EIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 333470564 652 TADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14599  251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 437-688 2.24e-55

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: 189.27  E-value: 2.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 437 RNNLAKNRYTDVLCYDHSRVVLSQEEDdpatdYINANFVD---GyKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMT 513
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPLGDEGG-----YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 514 TRVMERGRAKCGQYWePTEGGLAEYGSFRLRTMSIETN--EDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKA 591
Cdd:cd14597   75 TQEVEGGKIKCQRYW-PEILGKTTMVDNRLQLTLVRMQqlKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 592 MLNFLQRAREKqaemvralgdlwagHPRGpPIVVHCSAGIGRTGTFITLDIC---ISRLEDVgtaDIKGTVEKIRSQRAY 668
Cdd:cd14597  154 LLTFISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVlglISKDLDF---DISDIVRTMRLQRHG 215

                        250       260
                 ....*....|....*....|
gi 333470564 669 SIQMPDQYVFCHlALIEYAL 688
Cdd:cd14597  216 MVQTEDQYIFCY-QVILYVL 234
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 468-686 2.59e-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: 188.23  E-value: 2.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 468 DYINANFVD----GYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAEYGSFRL 543
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYW-PEPSGSSSYGGFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 544 RTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQaemvralgdlwAGHPRgpPI 623
Cdd:cd14601   80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR-----------AGKDE--PV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333470564 624 VVHCSAGIGRTGTFITLDICISRLE---DVGTADIkgtVEKIRSQRAYSIQMPDQYVF-CHLALIEY 686
Cdd:cd14601  147 VVHCSAGIGRTGVLITMETAMCLIEcnqPVYPLDI---VRTMRDQRAMMIQTPSQYRFvCEAILKVY 210
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 468-686 1.49e-54

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 185.98  E-value: 1.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 468 DYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLAeYGSFRLRTMS 547
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW-PSEGSVT-HGEITIEIKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMvralgdlwAGHprgpPIVVHC 627
Cdd:cd14622   79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--------GNH----PIVVHC 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 628 SAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14622  147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 439-683 6.59e-54

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: 187.45  E-value: 6.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 439 NLAKNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVME 518
Cdd:cd14604   57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 519 RGRAKCGQYWEPTEGGLAEYGSFRLRTMSIETNEDYTV--VELEIRNiktdEVRCVSHWQFTSWPDYGVPSSAKAMLNFL 596
Cdd:cd14604  137 MGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIrtLLLEFQN----ETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 597 QRAREKQAEmvralgdlwaghpRGPPIVVHCSAGIGRTGTFITLDICISRL------EDVGTADIkgtVEKIRSQRAYSI 670
Cdd:cd14604  213 SLMRKYQEH-------------EDVPICIHCSAGCGRTGAICAIDYTWNLLkagkipEEFNVFNL---IQEMRTQRHSAV 276

                        250
                 ....*....|...
gi 333470564 671 QMPDQYVFCHLAL 683
Cdd:cd14604  277 QTKEQYELVHRAI 289
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 442-685 1.62e-53

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: 184.27  E-value: 1.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 442 KNRYTDVLCYDHSRVVLSQEEDDPATDYINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGR 521
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 522 AKCGQYW-EPTEGGLaEYGSFRLRTMSIETNEDYTVVELEIRNIKtdEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAR 600
Cdd:cd14602   81 KKCERYWaEPGEMQL-EFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 601 EKQaemvralgdlwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAD---IKGTVEKIRSQRAYSIQMPDQYV 677
Cdd:cd14602  158 CYQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPEnfsVFSLIQEMRTQRPSLVQTKEQYE 224


                 ....*...
gi 333470564 678 FCHLALIE 685
Cdd:cd14602  225 LVYNAVIE 232
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 469-685 2.87e-53

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: 182.64  E-value: 2.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKN-AYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGlAEYGSFRLRTMS 547
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYW-PEEGS-EVYHIYEVHLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IET-NEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFlqraREKQAEMVRAlgdlwaghpRGPPIVVH 626
Cdd:cd14546   79 EHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEF----RRKVNKSYRG---------RSCPIVVH 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 627 CSAGIGRTGTFITLDICISRL-EDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14546  146 CSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 469-680 8.77e-53

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: 181.12  E-value: 8.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKN--AYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGR-AKCGQYWEPTEGGLAEYGSFRLRT 545
Cdd:cd17658    1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 546 MSIETNEDYTVVE-LEIRNIKTDE-VRCVSHWQFTSWPDYGVPSSAKAMLNFLQRarekqaemvralgdLWAGHPRGPPI 623
Cdd:cd17658   81 KKLKHSQHSITLRvLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLKR--------------LYGIPPSAGPI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 624 VVHCSAGIGRTGTFITLDICISR--LEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd17658  147 VVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 469-685 4.12e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 179.56  E-value: 4.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGY--KQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTM 546
Cdd:cd14596    1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 547 SIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREkqaemVRALGdlwaghprgpPIVVH 626
Cdd:cd14596   81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK-----VHNTG----------PIVVH 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 627 CSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14596  146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 442-680 1.31e-51

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: 178.57  E-value: 1.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 442 KNRYTDVLCYDHSRVVL-SQEEDDPATDYINANFVDGYK-QKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMER 519
Cdd:cd14611    2 KNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 520 GRaKCGQYWePTEGGLaeYGSFRLRTMSIETNEDYTVVELEIRNikTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRA 599
Cdd:cd14611   82 NE-KCVLYW-PEKRGI--YGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 600 REKQAEmvralgdlWAGhpRGPpIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFC 679
Cdd:cd14611  156 EEDRLA--------SPG--RGP-VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                 .
gi 333470564 680 H 680
Cdd:cd14611  225 H 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 469-680 1.52e-47

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: 166.83  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEPTEGGLAEYGSFRLRTMSI 548
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 E-TNEDYTVVELEIRniKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEmvralgdlwaghpRGPPIVVHC 627
Cdd:cd14542   81 KrVGPDFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGS-------------EDVPICVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 333470564 628 SAGIGRTGTFITLDICISRL------EDVGTADIkgtVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14542  146 SAGCGRTGTICAIDYVWNLLktgkipEEFSLFDL---VREMRKQRPAMVQTKEQYELVY 201
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 469-680 5.09e-47

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: 165.26  E-value: 5.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWEptEGGlAEYGSFRLRTMSI 548
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG--DEK-KTYGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQaemvralGDLWAGHPRGPPIVVHCS 628
Cdd:cd14558   78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 333470564 629 AGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14558  151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 469-680 2.44e-45

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: 160.63  E-value: 2.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNA-YISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGGLA-EYGSFRLRTM 546
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYW-PTERGQAlVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 547 SIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQRARE---KQAEMVRalgdlwaghprgpPI 623
Cdd:cd14539   80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQT-------------PI 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564 624 VVHCSAGIGRTGTFITLDICISRLE-DVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14539  147 VVHCSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 469-680 1.15e-44

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: 158.72  E-value: 1.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRvMERGRAKCGQYWePTEGGLAeYGSFRLRTMSI 548
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYW-PDEGSGT-YGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIKTDE--VRCVSHWQFTSWPDYG-VPSSAKAMLNFLQRAREKQAEMvralGDlwaghprgPPIVV 625
Cdd:cd14556   78 TIDEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS----GE--------GPIVV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333470564 626 HCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14556  146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 469-686 3.86e-41

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 149.74  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVD---GYKQKNaYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCGQYWePTEGG---LAEYGSFR 542
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYW-PRLGSrhnTVTYGRFK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 543 LRTMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSAKAMLNFLQrarekQAEMVRALGDLwAGHPRGP- 621
Cdd:cd14598   79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLE-----EIQSVRRHTNS-TIDPKSPn 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333470564 622 -PIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:cd14598  153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 572-685 1.11e-35

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: 130.17  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   572 VSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEmvralgdlwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 650
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 333470564   651 GTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
572-685 1.11e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 130.17  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   572 VSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEmvralgdlwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 650
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQ-----------SESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 333470564   651 GTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
432-690 6.43e-32

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 125.59  E-value: 6.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 432 THAKLRNNLAKNRYTDVLCYDHSRVvlsqEEDDPatdYINANFVDGyKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIV 511
Cdd:COG5599   35 QYLQNINGSPLNRFRDIQPYKETAL----RANLG---YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 512 MTTRVME--RGRAKCGQYWEPTEgglaEYGSFRLRTMSIET---NEDYTVVELEIRNIKTD-EVRCVSHWQFTSWPDYGV 585
Cdd:COG5599  107 VLASDDEisKPKVKMPVYFRQDG----EYGKYEVSSELTESiqlRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 586 PsSAKAMLNFLQRAREKQAEmvralgdlwAGHPRGPPiVVHCSAGIGRTGTFItLDICISRL---EDVGTADIKGTVEKI 662
Cdd:COG5599  183 I-SAEALKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSinaLVQITLSVEEIVIDM 250

                        250       260
                 ....*....|....*....|....*....
gi 333470564 663 RSQRAYSI-QMPDQYVFchlaLIEYALSR 690
Cdd:COG5599  251 RTSRNGGMvQTSEQLDV----LVKLAEQQ 275
CRAL_TRIO pfam00650
CRAL/TRIO domain;
83-226 3.98e-31

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 118.90  E-value: 3.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564   83 GKFTILPGRDASGAAIALFTANLHYPMTVTHKTTLQGVVYQLDVALQSS-ETQKAGLVFIYDMSTSKYSNFD---YDLSQ 158
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMpEGQVEGLTVIIDLKGLSLSNMDwwsISLLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564  159 KILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVF---TVSIPQLSLHVPRESLPVRLGG 226
Cdd:pfam00650  81 KIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVflkNSNEEELEKYIPPEQLPKEYGG 151
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 469-685 2.11e-30

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: 118.64  E-value: 2.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVmeRGRAKCGQYWepTEGGLAEYGSFRLRTMSI 548
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYW--PENGVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIK--TDEVRCVSHWQFTSWPDY-GVPSSAKAMLNFLQRAREKQAEMVRALGDlwaghprgppIVV 625
Cdd:cd14635   77 DLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGR----------TVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 626 HCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14635  147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 415-686 2.39e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 121.61  E-value: 2.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 415 LIREYTEIKARAPDGTFTHAKLRNNLAK--NRYTDVLCYDHSRVVLSQEEDdpatdYINANFVDGYKQKNAYISTQGPLP 492
Cdd:PHA02740  27 IIKEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKLFNDEK-----VLDARFVDGYDFEQKFICIINLCE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 493 KTSYDFWRMVWEQHCLLIVMTTRVMERgraKC-GQYWEPTEGGLAEYGSFRLRTMSIETNEDYTVVELEIRNIKTDEvRC 571
Cdd:PHA02740 102 DACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA-QK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 572 VSHWQFTSWPDYGVPSSAKAMLNFLQRAREKQAEMVRALGDLWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVG 651
Cdd:PHA02740 178 ISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIA-----PIIIDCIDGISSSAVFCVFDICATEFDKTG 252

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 333470564 652 TADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 686
Cdd:PHA02740 253 MLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 469-685 4.96e-29

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: 114.73  E-value: 4.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRvMERGRAkCGQYWEPTEGGLaeYGSFRLRTMSI 548
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWPEKTSCC--YGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 ETNEDYTVVELEIRNIK--TDEVRCVSHWQFTSWPDY-GVPSSAKAMLNFLQRAREKQAEmvralgdlWAGhpRGPPIVV 625
Cdd:cd14634   77 DIDEDIISRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQ--------YDG--REGRTVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 626 HCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14634  147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 469-685 1.39e-28

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: 113.46  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA-KCGQYWepTEGGLAEYGSFRLRTMS 547
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYW--PEPGLQQYGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IETNEDYTVVELEIRNIK--TDEVRCVSHWQFTSWPDY-GVPSSAKAMLNFLQRAREKQAEmvralgdlwAGHPRgppIV 624
Cdd:cd14637   79 GSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASVEKWQRE---------SGEGR---TV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564 625 VHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALIE 685
Cdd:cd14637  147 VHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 81-227 1.74e-28

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 111.66  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  81 ETGKFTILPGRDASGAAIALFTANLHYPMTVTHKTTLQGVVYQLDVALQSSETQKAGLVFIYDMSTSKYSNF-DYDLSQK 159
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 160 ILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS--IPQLSLHVPRESLPVRLGGT 227
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGGT 156
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 79-229 7.84e-28

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 109.70  E-value: 7.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564    79 ELETGKFTILPGR--DASGAAIALFTANLHYPMTVTHKTTLQGVVYQLD--VALQSSETQKAGLVFIYDMSTSKYSNFDY 154
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEkiLQEEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333470564   155 DLSQKILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS---IPQLSLHVPRESLPVRLGGTLE 229
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 469-678 1.75e-27

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: 110.10  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGraKCGQYWePTEGGLAEYGSFRLR---- 544
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYW-PTKEKPLECETFKVTlsge 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 545 -TMSIETNEDYTVVELEIRNIKTDEVRCVSHWQFTSWPDYGVPSSakAMLNFLQRAREKQAEmvralgdlwaghpRGPPI 623
Cdd:cd14550   78 dHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQ-------------RDGPI 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333470564 624 VVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVF 678
Cdd:cd14550  143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 469-680 3.62e-26

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: 106.65  E-value: 3.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRV-MERGrakCGQYWePTEGGLaEYGSFRLRTMS 547
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYW-PEEGML-RYGPIQVECMS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 548 IETNEDYTVVELEIRNIKTDE--VRCVSHWQFTSWPDY-GVPSSAKAMLNFLQRAREKQAEMVRALGDlwaghprgppIV 624
Cdd:cd14636   76 CSMDCDVISRIFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGR----------TI 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 333470564 625 VHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14636  146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 469-684 4.24e-19

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: 86.20  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRAKCgQYWePTEGGLAEYGSFRLRTMSI 548
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYW-PNKDEPINCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 549 E----TNEDYTVVE-LEIRNIKTDEVRCVSHWQFTSWPDYGVPSSakamlnflqrareKQAEMVRALGDLWAGhpRGPPI 623
Cdd:cd17669   79 EhkclSNEEKLIIQdFILEATQDDYVLEVRHFQCPKWPNPDSPIS-------------KTFELISIIKEEAAN--RDGPM 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333470564 624 VVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALI 684
Cdd:cd17669  144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 469-684 3.99e-18

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: 83.57  E-value: 3.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 469 YINANFVDGYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTtrvmergrakcgqywePTEGGLAE----YGSFRLR 544
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML----------------PDNQGLAEdefvYWPSREE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 545 TMSIET--------------NEDYTVV-ELEIRNIKTDEVRCVSHWQFTSWPDYGVP-SSAKAMLNFLqrareKQAEMVr 608
Cdd:cd17670   65 SMNCEAftvtliskdrlclsNEEQIIIhDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI-----KEEALT- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333470564 609 algdlwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIKGTVEKIRSQRAYSIQMPDQYVFCHLALI 684
Cdd:cd17670  139 ----------RDGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 141-232 2.04e-10

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 59.26  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564  141 IYDMS-TSKYSNFDYDLSQKILTLLKGGYPARLKKVLIVTAPLWFKAPFKIL-RLFVREKLRERVFTVS-IPQLSLHVPR 217
Cdd:pfam13716  45 VVDHTgVTSENFPSLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSsLSELWEGIDR 124

                          90
                  ....*....|....*
gi 333470564  218 ESLPVRLGGTLEVDH 232
Cdd:pfam13716 125 EQLPTELPGVLSYDE 139
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 619-680 4.23e-09

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: 54.66  E-value: 4.23e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333470564 619 RGPPIVVHCSAGIGRTGTFITLDICIsrledVGTADIKGTVEKIRSQR-AYSIQMPDQYVFCH 680
Cdd:cd14494   55 PGEPVLVHCKAGVGRTGTLVACYLVL-----LGGMSAEEAVRIVRLIRpGGIPQTIEQLDFLI 112
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
580-678 7.40e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.90  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 580 WPDYGVPSsakamlnflqrarekQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFItldICISRLEDVGTADIkgtV 659
Cdd:COG2453   55 IPDFGAPD---------------DEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVA---AAYLVLLGLSAEEA---L 113

                         90
                 ....*....|....*....
gi 333470564 660 EKIRSQRAYSIQMPDQYVF 678
Cdd:COG2453  114 ARVRAARPGAVETPAQRAF 132
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 443-677 2.58e-05

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 46.24  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 443 NRYTDVLCydhsrvvLSQEEDDPAtdyINANFVDgYKQKNAYISTQGPLPKTSYDFWRMVWEQHCLLIVMTTRVMERGRA 522
Cdd:cd14559    1 NRFTNIQT-------RVSTPVGKN---LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 523 KCGQYWEPTEgglaEYGSfrLRTMSIETNEDYTVVELEIR----NIKTDEVRC---VSHwqFTSWPDYGVPSSA--KAML 593
Cdd:cd14559   70 GLPPYFRQSG----TYGS--VTVKSKKTGKDELVDGLKADmynlKITDGNKTItipVVH--VTNWPDHTAISSEglKELA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 594 NFLQRAREKQAEMVRALGDLWAGHPRGPPIVVHCSAGIGRTGTFI-TLDICISR----LEDVgtadikgtVEKIRSQR-A 667
Cdd:cd14559  142 DLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAaAMELNKSPnnlsVEDI--------VSDMRTSRnG 213

                        250
                 ....*....|
gi 333470564 668 YSIQMPDQYV 677
Cdd:cd14559  214 KMVQKDEQLD 223
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 581-680 5.53e-05

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 44.18  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 581 PDYGVPSSAKAMLNFLQrarekqaEMVRALGDlwaghprGPPIVVHCSAGIGRTGTfitldICISRLEDVG-TADIKGTV 659
Cdd:cd14505   81 PDGGVPSDIAQWQELLE-------ELLSALEN-------GKKVLIHCKGGLGRTGL-----IAACLLLELGdTLDPEQAI 141

                         90       100
                 ....*....|....*....|.
gi 333470564 660 EKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14505  142 AAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 581-689 7.03e-05

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: 43.42  E-value: 7.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 581 PDYGVPSsakamlnflqraREKQAEMVRALGDLWAghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAdikgtVE 660
Cdd:cd14504   58 EDYTPPT------------LEQIDEFLDIVEEANA---KNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDA-----IN 117

                         90       100
                 ....*....|....*....|....*....
gi 333470564 661 KIRSQRAYSIQMPDQYVFchlaLIEYALS 689
Cdd:cd14504  118 EIRRIRPGSIETSEQEKF----VIQFAKT 142
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 572-680 3.89e-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: 42.34  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333470564 572 VSHWQFtSWPDYGVPSSAKAMlnflqrarekqaEMVRALgdlwAGHPR-GPPIVVHCSAGIGRTGTFITldiCI-SRLED 649
Cdd:cd14506   77 IYFYNF-GWKDYGVPSLTTIL------------DIVKVM----AFALQeGGKVAVHCHAGLGRTGVLIA---CYlVYALR 136

                         90       100       110
                 ....*....|....*....|....*....|.
gi 333470564 650 VGTADikgTVEKIRSQRAYSIQMPDQYVFCH 680
Cdd:cd14506  137 MSADQ---AIRLVRSKRPNSIQTRGQVLCVR 164
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH