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Conserved domains on  [gi|528520972|ref|XP_005163030|]
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tyrosine-protein phosphatase non-receptor type 9 [Danio rerio]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 13931872)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins

Graphical summary

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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 ...
 286-554 0e+00

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: 578.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 286 QRSGIYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARR-NERSDYINASFMDGYKQKNAYIGTQGP 364
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNgDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 365 LEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQR 444
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 445 QVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDV 524
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 528520972 525 GTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 81-231 1.07e-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: 111.62  E-value: 1.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972    81 ELLSGKFTVLGVR--DPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 156
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972   157 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMA---DLRQHLPRDCLPEHLGGCLP 231
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDskeELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
11-59 3.95e-07

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.95e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 528520972    11 EQATKQFLEEINKWTSQHgVSPLSWDVAVKFLMARKFDVLRAIELFHSY 59
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 286-554 0e+00

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: 578.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 286 QRSGIYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARR-NERSDYINASFMDGYKQKNAYIGTQGP 364
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNgDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 365 LEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQR 444
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 445 QVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDV 524
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 528520972 525 GTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
289-559 1.61e-123

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 363.90  E-value: 1.61e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   289 GIYLEYEELRREQPP-GTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNERSDYINASFMDGYKQKNAYIGTQGPLEK 367
Cdd:smart00194   1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   368 TYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVT 447
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   448 HFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTL 527
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQS-------------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 528520972   528 NICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
314-559 1.31e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 339.99  E-value: 1.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  314 NQERNRYGDVLCLDQTRVRLKARrNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEG 393
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGD-PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  394 GRRKCGQYWPQEEGGQEVYGYIAVVNHR-VDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGA 472
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  473 VKhqqqwavqafgtQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:pfam00102 160 VR------------KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                  ....*..
gi 528520972  553 CHAAILE 559
Cdd:pfam00102 228 LYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 271-557 5.89e-72

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 233.28  E-value: 5.89e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 271 EAMSLAELMAHLNRAQ-RSGIYLEYEELRREQPPGTFTCALAahNQERNRYGDVLCLDQTRVRLKARRNeRSDYINASFM 349
Cdd:PHA02738   7 RELKYAEFLALMEKSDcEEVITREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERN-RGDYINANYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 350 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYN 429
Cdd:PHA02738  84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 430 QTTLELHNTETFEQrQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKH-QQQWAVQAF--GTQwRGHPlgPPMVVHCSAGIG 506
Cdd:PHA02738 164 KSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcQKELAQESLqiGHN-RLQP--PPIVVHCNAGLG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528520972 507 RTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:PHA02738 240 RTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
317-550 8.84e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.52  E-value: 8.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKARrnersdYINASFMDGyKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:COG5599   45 LNRFRDIQPYKETALRANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 --KCGQYWPQeeggQEVYGYIAVVNHRVDNHahYNQTTLELHnteTF---------EQRQVTHFQFLSWPDYGVPSSAVs 465
Cdd:COG5599  118 kvKMPVYFRQ----DGEYGKYEVSSELTESI--QLRDGIEAR---TYvltikgtgqKKIEIPVLHVKNWPDHGAISAEA- 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 466 LIDFLGAVKHQQQWavqafgtqwRGHPLGPPmVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNICQTVRRMRSQRAF 542
Cdd:COG5599  188 LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDMRTSRNG 256


                 ....*....
gi 528520972 543 SI-QTPEQY 550
Cdd:COG5599  257 GMvQTSEQL 265
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 81-231 1.07e-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: 111.62  E-value: 1.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972    81 ELLSGKFTVLGVR--DPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 156
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972   157 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMA---DLRQHLPRDCLPEHLGGCLP 231
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDskeELLEYIDKEQLPEELGGTLD 158
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 83-228 2.64e-27

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: 107.81  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  83 LSGKFTVLGVRDPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSNYTNF-ELDLSKK 161
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 162 ILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK--MADLRQHLPRDCLPEHLGG 228
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGG 155
CRAL_TRIO pfam00650
CRAL/TRIO domain;
84-228 7.33e-25

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 100.79  E-value: 7.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   84 SGKFTVLGvRDPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSNYTNFE---LDLS 159
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972  160 KKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK---MADLRQHLPRDCLPEHLGG 228
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
11-59 3.95e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.95e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 528520972    11 EQATKQFLEEINKWTSQHgVSPLSWDVAVKFLMARKFDVLRAIELFHSY 59
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 286-554 0e+00

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: 578.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 286 QRSGIYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARR-NERSDYINASFMDGYKQKNAYIGTQGP 364
Cdd:cd14543    1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNgDERTDYINANFMDGYKQKNAYIATQGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 365 LEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQR 444
Cdd:cd14543   81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 445 QVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDV 524
Cdd:cd14543  161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 528520972 525 GTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14543  241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
289-559 1.61e-123

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 363.90  E-value: 1.61e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   289 GIYLEYEELRREQPP-GTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNERSDYINASFMDGYKQKNAYIGTQGPLEK 367
Cdd:smart00194   1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   368 TYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVT 447
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   448 HFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTL 527
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQS-------------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 528520972   528 NICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
314-559 1.31e-114

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 339.99  E-value: 1.31e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  314 NQERNRYGDVLCLDQTRVRLKARrNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEG 393
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGD-PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  394 GRRKCGQYWPQEEGGQEVYGYIAVVNHR-VDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGA 472
Cdd:pfam00102  80 GREKCAQYWPEEEGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  473 VKhqqqwavqafgtQWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:pfam00102 160 VR------------KSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIF 227


                  ....*..
gi 528520972  553 CHAAILE 559
Cdd:pfam00102 228 LYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 343-554 4.83e-94

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: 286.10  E-value: 4.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRV 422
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCS 502
Cdd:cd00047   81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR-------------KPNGPIVVHCS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528520972 503 AGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd00047  148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 313-559 1.09e-83

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: 260.79  E-value: 1.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 313 HNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTD 391
Cdd:cd14553    2 VNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 392 EGGRRKCGQYWPQEegGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLG 471
Cdd:cd14553   82 ERSRVKCDQYWPTR--GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 472 AVKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYY 551
Cdd:cd14553  160 RVKACNP-------------PDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226


                 ....*...
gi 528520972 552 FCHAAILE 559
Cdd:cd14553  227 FIHDALLE 234
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 343-554 1.68e-75

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: 238.40  E-value: 1.68e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRV 422
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE--GTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETF------EQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhqqqwavqafgtqwRGHPLGP- 495
Cdd:cd14549   79 EVLATYTVRTFSLKNLKLKkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSS--------------AANPPGAg 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 496 PMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14549  145 PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 319-554 5.79e-74

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: 234.94  E-value: 5.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 319 RYGDVLCLDQTRVRLKARRNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRK 397
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 398 CGQYWPQEEgGQEVYGYIAVvnHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhqq 477
Cdd:cd14548   81 CDHYWPFDQ-DPVYYGDITV--TMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVR--- 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528520972 478 qwavqafgtQWRGHPLGpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14548  155 ---------DYIKQEKG-PTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 314-558 4.52e-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: 233.19  E-value: 4.52e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEEGGQevYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGa 472
Cdd:cd14554   86 MGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIG- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 473 vkhQQQWAVQAFGTQwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14554  163 ---QVHKTKEQFGQE-------GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQF 232


                 ....*.
gi 528520972 553 CHAAIL 558
Cdd:cd14554  233 CYRAAL 238
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 343-554 5.26e-72

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: 229.44  E-value: 5.26e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMD-GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPqEEGGQEVYGYIAV--VN 419
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP-SGEYEGEYGDLTVelVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 420 HRVDNHAHYNQTTLELHnTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrGHPLGPPMVV 499
Cdd:cd18533   80 EEENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELND-----------SASLDPPIIV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528520972 500 HCSAGIGRTGTFCALDICLSQLQDVGTLN---------ICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd18533  148 HCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PHA02738 PHA02738
hypothetical protein; Provisional
 271-557 5.89e-72

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 233.28  E-value: 5.89e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 271 EAMSLAELMAHLNRAQ-RSGIYLEYEELRREQPPGTFTCALAahNQERNRYGDVLCLDQTRVRLKARRNeRSDYINASFM 349
Cdd:PHA02738   7 RELKYAEFLALMEKSDcEEVITREHQKVISEKVDGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERN-RGDYINANYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 350 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYN 429
Cdd:PHA02738  84 DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 430 QTTLELHNTETFEQrQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKH-QQQWAVQAF--GTQwRGHPlgPPMVVHCSAGIG 506
Cdd:PHA02738 164 KSTLLLTDGTSATQ-TVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQcQKELAQESLqiGHN-RLQP--PPIVVHCNAGLG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528520972 507 RTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:PHA02738 240 RTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 293-559 3.88e-70

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: 226.84  E-value: 3.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 293 EYEELRREQPPGTFTCALAAH--NQERNRYGDVLCLDQTRVRLK---ARRNERSDYINASFMDGYKQKNAYIGTQGPLEK 367
Cdd:cd17667    4 DFEEVQRCTADMNITAEHSNHpdNKHKNRYINILAYDHSRVKLRplpGKDSKHSDYINANYVDGYNKAKAYIATQGPLKS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 368 TYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEggQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFE----- 442
Cdd:cd17667   84 TFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkgn 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 443 ------QRQVTHFQFLSWPDYGVPSSAVSLIDFLgavkhQQQWAVQAfgtqwrghPLGPPMVVHCSAGIGRTGTFCALDI 516
Cdd:cd17667  162 pkgrqnERTVIQYHYTQWPDMGVPEYALPVLTFV-----RRSSAART--------PEMGPVLVHCSAGVGRTGTYIVIDS 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 528520972 517 CLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd17667  229 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 314-561 6.12e-70

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: 226.46  E-value: 6.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEegGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGA 472
Cdd:cd14626  121 KSRVKCDQYWPIR--GTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRR 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 473 VKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14626  199 VKACNP-------------PDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIF 265


                 ....*....
gi 528520972 553 CHAAILEHA 561
Cdd:cd14626  266 IHEALLEAA 274
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 317-554 1.16e-68

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: 221.50  E-value: 1.16e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKARrNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLK-QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 KCGQYWPQEEGgqevYGYI------AVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFL 470
Cdd:cd14545   80 KCAQYWPQGEG----NAMIfedtglKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 471 GAVKHQqqwavqafGTQWRGHplGPPmVVHCSAGIGRTGTFCALDICLSQL--QDVGTLNICQTVRRMRSQRAFSIQTPE 548
Cdd:cd14545  156 QKVRES--------GSLSSDV--GPP-VVHCSAGIGRSGTFCLVDTCLVLIekGNPSSVDVKKVLLEMRKYRMGLIQTPD 224


                 ....*.
gi 528520972 549 QYYFCH 554
Cdd:cd14545  225 QLRFSY 230
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 277-558 6.71e-67

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: 218.57  E-value: 6.71e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 277 ELMAHLNRAQRSG-IYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLkarrNERSDYINASFMD----G 351
Cdd:cd14600    2 ESMAQLKKGLESGtVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNmeipS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 352 YKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEeggQEV--YGYIAVVNHRVDNHAHYN 429
Cdd:cd14600   78 ANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDP---PDVmeYGGFRVQCHSEDCTIAYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 430 QTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVqafgtqwrghplgpPMVVHCSAGIGRTG 509
Cdd:cd14600  155 FREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE--------------PVLVHCSAGIGRTG 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528520972 510 TFCALD--ICLSQL-QDVGTLNIcqtVRRMRSQRAFSIQTPEQYYFCHAAIL 558
Cdd:cd14600  221 VLVTMEtaMCLTERnQPVYPLDI---VRKMRDQRAMMVQTSSQYKFVCEAIL 269
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 293-562 1.20e-66

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 218.72  E-value: 1.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 293 EYEELRREQPPgtFTC--ALAAHNQERNRYGDVLCLDQTRVRLKARRNeRSDYINASFMDGYKQKNAYIGTQGPLEKTYG 370
Cdd:PHA02742  31 EHEHIMQEIVA--FSCneSLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 371 DFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQ 450
Cdd:PHA02742 108 DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 451 FLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHPlgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNIC 530
Cdd:PHA02742 188 YEDWPHGGLPRDPNKFLDFVLAVREADLKADVDIKGENIVKE--PPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265

                        250       260       270
                 ....*....|....*....|....*....|..
gi 528520972 531 QTVRRMRSQRAFSIQTPEQYYFCHAAILEHAQ 562
Cdd:PHA02742 266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 268-559 5.24e-66

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: 216.50  E-value: 5.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 268 PGAEAMSLAELMAHLNRAQRSGIYLEYEELrreQPPGTFTCALA--AHNQERNRYGDVLCLDQTRVRLKARRN-ERSDYI 344
Cdd:cd14625    2 PPIPISELAEHTERLKANDNLKLSQEYESI---DPGQQFTWEHSnlEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 345 NASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRVDN 424
Cdd:cd14625   79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSR--GTETYGMIQVTLLDTIE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 425 HAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCSAG 504
Cdd:cd14625  157 LATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNP-------------PDAGPIVVHCSAG 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528520972 505 IGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14625  224 VGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 314-562 9.99e-65

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: 211.94  E-value: 9.99e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRNER--SDYINASFM-------DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVI 384
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 385 VMTTRTDEGGRRKCGQYWPqEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNT-ETFEQRQVTHFQFLSWPDYGVPSSA 463
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWP-DEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 464 VSLIDFLGAVKHQQQWAVQAfgtqwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVG---TLNICQTVRRMRSQR 540
Cdd:cd14544  160 GGVLNFLEDVNQRQESLPHA-----------GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQR 228

                        250       260
                 ....*....|....*....|..
gi 528520972 541 AFSIQTPEQYYFCHAAILEHAQ 562
Cdd:cd14544  229 SGMVQTEAQYKFIYVAVAQYIE 250
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 294-562 1.48e-64

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: 212.58  E-value: 1.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 294 YEELRREQppGTFTCALAAH--NQERNRYGDVLCLDQTRVRLKARRNersDYINASFMDGYKQKNAYIGTQGPLEKTYGD 371
Cdd:cd14608    5 YQDIRHEA--SDFPCRVAKLpkNKNRNRYRDVSPFDHSRIKLHQEDN---DYINASLIKMEEAQRSYILTQGPLPNTCGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 372 FWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYgyiAVVNHRV-----DNHAHYNQTTLELHNTETFEQRQV 446
Cdd:cd14608   80 FWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIF---EDTNLKLtliseDIKSYYTVRQLELENLTTQETREI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 447 THFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAvqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICL---SQLQD 523
Cdd:cd14608  157 LHFHYTTWPDFGVPESPASFLNFLFKVRESGSLS-----------PEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKD 225

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 528520972 524 VGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEHAQ 562
Cdd:cd14608  226 PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAK 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 343-557 2.77e-64

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: 209.05  E-value: 2.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRV 422
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED--GSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrgHPLGPPMVVHCS 502
Cdd:cd14552   79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ------------QSGNHPITVHCS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528520972 503 AGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:cd14552  147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 288-560 1.03e-63

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: 210.74  E-value: 1.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 288 SGIYLEYEELRREQPPGT-FTCALAAHNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPL 365
Cdd:cd14627   26 TGMELEFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 366 EKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQevYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQ 445
Cdd:cd14627  106 AETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 446 VTHFQFLSWPDYGVPSSAVSLIDFLGAVkHQQQwavQAFGTQwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVG 525
Cdd:cd14627  184 VRQFQFTDWPEQGVPKSGEGFIDFIGQV-HKTK---EQFGQD-------GPISVHCSAGVGRTGVFITLSIVLERMRYEG 252

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528520972 526 TLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEH 560
Cdd:cd14627  253 VVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 314-559 1.33e-63

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: 208.73  E-value: 1.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKA-RRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14630    3 NRNKNRYGNIISYDHSRVRLQLlDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEeggQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGA 472
Cdd:cd14630   83 VGRVKCVRYWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 473 VKhqqqwavqafgtqWRGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14630  160 VK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226


                 ....*..
gi 528520972 553 CHAAILE 559
Cdd:cd14630  227 VHDAILE 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 318-554 1.99e-63

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: 207.63  E-value: 1.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKN-AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGgR 395
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDdPLSSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 396 RKCGQYWPQEEGgqEVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVkh 475
Cdd:cd14547   80 EKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEV-- 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 476 qQQWAVQAFGTqwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14547  154 -EEARQTEPHR--------GPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 271-557 4.36e-63

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 210.27  E-value: 4.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 271 EAMSLAELMAHLNRAQR-SGIYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKAR------------- 336
Cdd:PHA02746   7 EIFNAFDFFDKTNHAKFcEFVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAHeslkmfdvgdsdg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 337 -------RNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGgRRKCGQYWPQEEGGQ 409
Cdd:PHA02746  87 kkievtsEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDD-DEKCFELWTKEEDSE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 410 EVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQwr 489
Cdd:PHA02746 166 LAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIKQADND-- 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972 490 GHPLGPpMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:PHA02746 244 PQTLGP-IVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 290-552 4.62e-63

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 209.86  E-value: 4.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 290 IYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNERSDYINASFMDGYKQKNAYIGTQGPLEKTY 369
Cdd:PHA02747  27 IRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 370 GDFWRMVWEQNVLVIVMTTRTDE-GGRRKCGQYW-PQEEGGQEVYGY-IAVVNHRVdnHAHYNQTTLELHNTETFEQRQV 446
Cdd:PHA02747 107 ADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWcLNEDGNIDMEDFrIETLKTSV--RAKYILTLIEITDKILKDSRKI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 447 THFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGT 526
Cdd:PHA02747 185 SHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLFNPK---DALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKA 261

                        250       260
                 ....*....|....*....|....*.
gi 528520972 527 LNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:PHA02747 262 ICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 273-559 1.15e-62

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: 207.66  E-value: 1.15e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 273 MSLAELMAHLNRAQRSGIYLEYEELRREQPPGTFTCALA--AHNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFM 349
Cdd:cd14624    4 IPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSnlEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 350 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRVDNHAHYN 429
Cdd:cd14624   84 DGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR--GTETYGLIQVTLLDTVELATYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 430 QTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTG 509
Cdd:cd14624  162 VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNP-------------PDAGPMVVHCSAGVGRTG 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 528520972 510 TFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14624  229 CFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 330-559 2.20e-62

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: 204.89  E-value: 2.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 330 RVRLKARRNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegG 408
Cdd:cd14623   12 RVIIPVKRGEEnTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSD--G 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 409 QEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtQW 488
Cdd:cd14623   90 SVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ--------QS 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528520972 489 RGHplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14623  162 GNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 288-560 2.50e-62

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: 207.28  E-value: 2.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 288 SGIYLEYEELRREQPPGT-FTCALAAHNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPL 365
Cdd:cd14628   25 TGMELEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 366 EKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQevYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQ 445
Cdd:cd14628  105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 446 VTHFQFLSWPDYGVPSSAVSLIDFLGAVkHQQQwavQAFGTQwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVG 525
Cdd:cd14628  183 VRQFQFTDWPEQGVPKSGEGFIDFIGQV-HKTK---EQFGQD-------GPISVHCSAGVGRTGVFITLSIVLERMRYEG 251

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528520972 526 TLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEH 560
Cdd:cd14628  252 VVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 318-552 2.78e-62

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: 204.67  E-value: 2.78e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKARRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRK 397
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 398 CGQYWPQEegGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVK-HQ 476
Cdd:cd14615   81 CEEYWPSK--QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVReYM 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528520972 477 QQwavqafgtqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14615  159 KQ------------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 318-559 2.97e-62

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: 204.74  E-value: 2.97e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKA-RRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPiHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 KCGQYWPQEEgGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhq 476
Cdd:cd14619   81 KCEHYWPLDY-TPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR-- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 477 qQWAVQAFGTqwrghplGPPmVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAA 556
Cdd:cd14619  158 -QWLDQTMSG-------GPT-VVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQC 228


                 ...
gi 528520972 557 ILE 559
Cdd:cd14619  229 ILD 231
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 343-558 6.85e-62

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: 202.90  E-value: 6.85e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRV 422
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD--GSEEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFE--------QRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQqqwavqafgtqwRGHPLG 494
Cdd:cd17668   79 QVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYA------------KRHAVG 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528520972 495 pPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAIL 558
Cdd:cd17668  147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 342-558 4.65e-61

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: 201.02  E-value: 4.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 342 DYINASFMD----GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPqEEGGQEVYGYIAV 417
Cdd:cd14541    1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQFGNLQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 418 VNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVqafgtqwrghplgPPM 497
Cdd:cd14541   80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV-------------EPT 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528520972 498 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIcqtVRRMRSQRAFSIQTPEQYYFCHAAIL 558
Cdd:cd14541  147 VVHCSAGIGRTGVLITMEtaMCLIEAnEPVYPLDI---VRTMRDQRAMLIQTPSQYRFVCEAIL 207
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 314-560 2.72e-60

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: 201.88  E-value: 2.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14629   53 NKFKNRLVNIMPYELTRVCLQPIRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEEGGQevYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGA 472
Cdd:cd14629  133 MGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 473 VkHQQQwavQAFGTQwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14629  211 V-HKTK---EQFGQD-------GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQL 279


                 ....*...
gi 528520972 553 CHAAILEH 560
Cdd:cd14629  280 CYRAALEY 287
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 318-558 5.40e-60

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: 198.63  E-value: 5.40e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKARRNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 KCGQYWPQEEgGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQ 476
Cdd:cd14618   81 LCDHYWPSES-TPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 477 QQwavqafGTQWRGhplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAA 556
Cdd:cd14618  160 VQ------ATKGKG-----PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                 ..
gi 528520972 557 IL 558
Cdd:cd14618  229 IL 230
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 343-554 3.00e-59

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: 195.82  E-value: 3.00e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRV 422
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLEL-HNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFlgavkhqqQWAVQAFGTQWRGhplgpPMVVHC 501
Cdd:cd14557   81 KICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKL--------RRRVNAFNNFFSG-----PIVVHC 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528520972 502 SAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14557  148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 343-559 3.73e-59

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: 195.67  E-value: 3.73e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFM--DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWP-QEEGGQEVYGYIAVVN 419
Cdd:cd14538    1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 420 HRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHqqqwavqaFGTQWrghplgpPMVV 499
Cdd:cd14538   81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--------IHNSG-------PIVV 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 500 HCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14538  146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 277-559 7.56e-59

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: 197.19  E-value: 7.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 277 ELMAHLNR---AQRSGIYLEYEELRREQPpGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNER-SDYINASFMDGY 352
Cdd:cd14633    1 DLLQHITQmkcAEGYGFKEEYESFFEGQS-APWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 353 KQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEeggQEVYGYIAVVNHRVDNHAHYNQTT 432
Cdd:cd14633   80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 433 LELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCSAGIGRTGTFC 512
Cdd:cd14633  157 FAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP-------------PNAGPLVVHCSAGAGRTGCFI 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 528520972 513 ALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14633  224 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 294-557 2.29e-58

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: 195.57  E-value: 2.29e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 294 YEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKarrNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFW 373
Cdd:cd14607    4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 374 RMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEggQEVYGY----IAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHF 449
Cdd:cd14607   81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDE--EEVLSFketgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 450 QFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghpLGP---PMVVHCSAGIGRTGTFCALDICLSQLQ--DV 524
Cdd:cd14607  159 HYTTWPDFGVPESPASFLNFLFKVRESGS--------------LSPehgPAVVHCSAGIGRSGTFSLVDTCLVLMEkkDP 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 528520972 525 GTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:cd14607  225 DSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 314-559 2.41e-58

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: 195.81  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14603   30 NVKKNRYKDILPYDQTRVILSLLQEEgHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEEGGQEvYGYIAVVN---HRVDNHAHYNQTTLELHNtetfEQRQVTHFQFLSWPDYGVPSSAVSLIDF 469
Cdd:cd14603  110 MGKKKCERYWAQEQEPLQ-TGPFTITLvkeKRLNEEVILRTLKVTFQK----ESRSVSHFQYMAWPDHGIPDSPDCMLAM 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 470 LGAVKHQQQWAVQafgtqwrghplgpPMVVHCSAGIGRTGTFCALD-----ICLSQLQDvgTLNICQTVRRMRSQRAFSI 544
Cdd:cd14603  185 IELARRLQGSGPE-------------PLCVHCSAGCGRTGVICTVDyvrqlLLTQRIPP--DFSIFDVVLEMRKQRPAAV 249

                        250
                 ....*....|....*
gi 528520972 545 QTPEQYYFCHAAILE 559
Cdd:cd14603  250 QTEEQYEFLYHTVAQ 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 314-564 3.90e-58

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: 196.31  E-value: 3.90e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKAR-RNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14604   57 NVKKNRYKDILPFDHSRVKLTLKtSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEEGGQEVYG--YIAVVNHRVDNHAHYNQTTLELHNtetfEQRQVTHFQFLSWPDYGVPSSAVSLIDFL 470
Cdd:cd14604  137 MGRKKCERYWPLYGEEPMTFGpfRISCEAEQARTDYFIRTLLLEFQN----ETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 471 GAVKHQQQwavqafgtqwrgHPlGPPMVVHCSAGIGRTGTFCALDICLSQLQdVGTL----NICQTVRRMRSQRAFSIQT 546
Cdd:cd14604  213 SLMRKYQE------------HE-DVPICIHCSAGCGRTGAICAIDYTWNLLK-AGKIpeefNVFNLIQEMRTQRHSAVQT 278

                        250
                 ....*....|....*...
gi 528520972 547 PEQYYFCHAAILEHAQRQ 564
Cdd:cd14604  279 KEQYELVHRAIAQLFEKQ 296
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 314-557 5.88e-58

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: 194.08  E-value: 5.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRL-KARRNER-SDYINASFM--------DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLV 383
Cdd:cd14605    2 NKNKNRYKNILPFDHTRVVLhDGDPNEPvSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 384 IVMTTRTDEGGRRKCGQYWPQEEGGQEvYGYIAVVNHRvDNHAH-YNQTTLELH-----NTEtfeqRQVTHFQFLSWPDY 457
Cdd:cd14605   82 IVMTTKEVERGKSKCVKYWPDEYALKE-YGVMRVRNVK-ESAAHdYILRELKLSkvgqgNTE----RTVWQYHFRTWPDH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 458 GVPSSAVSLIDFLGAVKHQQQWAVQAfgtqwrghplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNICQTVR 534
Cdd:cd14605  156 GVPSDPGGVLDFLEEVHHKQESIMDA-----------GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQ 224

                        250       260
                 ....*....|....*....|...
gi 528520972 535 RMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:cd14605  225 MVRSQRSGMVQTEAQYRFIYMAV 247
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 314-559 8.09e-58

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: 194.33  E-value: 8.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRNER--SDYINASFM------DGYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIV 385
Cdd:cd14606   18 NKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRVIV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 386 MTTRTDEGGRRKCGQYWPqEEGGQEVYGYIAVVNHRVDNHAHYNQTTLEL---HNTETFeqRQVTHFQFLSWPDYGVPSS 462
Cdd:cd14606   97 MTTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELI--REIWHYQYLSWPDHGVPSE 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 463 AVSLIDFLGAVKHQQQwavqafgtqwrGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGT---LNICQTVRRMRSQ 539
Cdd:cd14606  174 PGGVLSFLDQINQRQE-----------SLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQ 242

                        250       260
                 ....*....|....*....|
gi 528520972 540 RAFSIQTPEQYYFCHAAILE 559
Cdd:cd14606  243 RSGMVQTEAQYKFIYVAIAQ 262
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 314-558 8.30e-57

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: 190.43  E-value: 8.30e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLkarrNERSDYINASF--MDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTD 391
Cdd:cd14597    3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 392 EGGRRKCGQYWPQEEGGQEVYG---YIAVVN-HRVDNhahYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLI 467
Cdd:cd14597   79 EGGKIKCQRYWPEILGKTTMVDnrlQLTLVRmQQLKN---FVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 468 DFLGAVKHQqqwavqafgtqwrgHPLGpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTP 547
Cdd:cd14597  156 TFISYMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTE 220

                        250
                 ....*....|.
gi 528520972 548 EQYYFCHAAIL 558
Cdd:cd14597  221 DQYIFCYQVIL 231
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 273-559 8.37e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 192.19  E-value: 8.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 273 MSLAELMAHLNRAQRsgIYLEYEELRREQP-PGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNE-RSDYINAS-FM 349
Cdd:cd14610    4 MILSYMEDHLKNKNR--LEKEWEALCAYQAePNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHsHSDYINASpIM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 350 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYgYIAVVNhRVDNH---A 426
Cdd:cd14610   82 DHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDE--GSNLY-HIYEVN-LVSEHiwcE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 427 HYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhqqqwavqafgTQWRGHPLgpPMVVHCSAGIG 506
Cdd:cd14610  158 DFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVN-----------KCYRGRSC--PIIVHCSDGAG 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528520972 507 RTGTFCALDICLSQL-QDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14610  225 RSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 343-559 2.73e-56

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: 188.20  E-value: 2.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEeggQEVYGYIAVVNHRV 422
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD---TEVYGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCS 502
Cdd:cd14555   78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP-------------PSAGPIVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528520972 503 AGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14555  145 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 303-560 1.56e-55

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: 189.46  E-value: 1.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 303 PGTFTCALAA--HNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQ 379
Cdd:cd14621   39 PIQATCEAASkeENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 380 NVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRVDNHAHYNQTTLELHN----TETFEQRQVTHFQFLSWP 455
Cdd:cd14621  119 NTATIVMVTNLKERKECKCAQYWPDQ--GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWP 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 456 DYGVPSSAVSLIDFLGAVKhqqqwavqAFGTQWRGhplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRR 535
Cdd:cd14621  197 DFGVPFTPIGMLKFLKKVK--------NCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSR 263

                        250       260
                 ....*....|....*....|....*
gi 528520972 536 MRSQRAFSIQTPEQYYFCHAAILEH 560
Cdd:cd14621  264 IRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 343-552 2.56e-55

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: 185.50  E-value: 2.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHRV 422
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQ--GCWTYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTL----ELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhqqqwavqAFGTQWRGhplgpPMV 498
Cdd:cd14551   79 VVLVDYTTRKFciqkVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVK--------SANPPRAG-----PIV 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528520972 499 VHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14551  146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 343-554 2.95e-55

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: 185.28  E-value: 2.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNA-YIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHR 421
Cdd:cd14539    1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 422 VDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVK--HQQQwavqafgtqwrgHPLGPPMVV 499
Cdd:cd14539   81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshYLQQ------------RSLQTPIVV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 500 HCSAGIGRTGTFCALdicLSQLQDV----GTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14539  149 HCSSGVGRTGAFCLL---YAAVQEIeagnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 317-554 2.96e-55

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: 186.97  E-value: 2.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKAR--RNERSDYINASFMDGYKQK-NAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEG 393
Cdd:cd14612   18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 394 gRRKCGQYWPQEEGgqeVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAV 473
Cdd:cd14612   98 -KEKCVHYWPEKEG---TYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 474 KHQQQWAvqafgtqwrGHPlgPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFC 553
Cdd:cd14612  172 EESRQTA---------ASP--GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240


                 .
gi 528520972 554 H 554
Cdd:cd14612  241 H 241
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 343-561 9.12e-55

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: 184.58  E-value: 9.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINAS---FMDGYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQ--EVYGYIAV 417
Cdd:cd14540    1 YINAShitATVGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaLTFGEYKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 418 VNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRghplGPPM 497
Cdd:cd14540   80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNR----NPPT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528520972 498 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEHA 561
Cdd:cd14540  156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 343-559 1.15e-54

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: 183.80  E-value: 1.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKN-AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVvnHR 421
Cdd:cd14546    1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEE--GSEVYHIYEV--HL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 422 VDNH---AHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQqwavqafgtqwRGhpLGPPMV 498
Cdd:cd14546   77 VSEHiwcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY-----------RG--RSCPIV 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972 499 VHCSAGIGRTGTFCALDICLSQL-QDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14546  144 VHCSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 318-554 1.61e-54

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: 184.35  E-value: 1.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKARRNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 KCGQYWPQEeggQEVYGYIAVVNHRVDNHAHYNQTTLELH--NTETFE-QRQVTHFQFLSWPDYGVPSSAVSLIDFLGAV 473
Cdd:cd14617   81 KCDHYWPAD---QDSLYYGDLIVQMLSESVLPEWTIREFKicSEEQLDaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 474 KHQQQWAvqafgtqwrghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFC 553
Cdd:cd14617  158 RDYINRT-----------PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYL 226


                 .
gi 528520972 554 H 554
Cdd:cd14617  227 H 227
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 343-554 2.51e-54

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: 182.98  E-value: 2.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEeggQEVYGYIAVVNHRV 422
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDE---KKTYGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQqwavqafGTQWRGHPLGPPMVVHCS 502
Cdd:cd14558   78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528520972 503 AGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14558  151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 343-559 5.55e-54

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: 182.17  E-value: 5.55e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEeggQEVYGYIAVVNHRV 422
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD---SDTYGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrghPLGPPMVVHCS 502
Cdd:cd14632   78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP-------------PDAGPVVVHCS 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528520972 503 AGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14632  145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 320-559 8.77e-54

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: 182.45  E-value: 8.77e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 320 YGDVLCLDQTRVRL-KARRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKC 398
Cdd:cd14620    1 YPNILPYDHSRVILsQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 399 GQYWPQEegGQEVYGYIAV--------VNHRVDNHAHYNQttlelHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFL 470
Cdd:cd14620   81 YQYWPDQ--GCWTYGNIRVavedcvvlVDYTIRKFCIQPQ-----LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 471 GAVKHqqqwavqafgtqwrghpLGP----PMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQT 546
Cdd:cd14620  154 KKVKS-----------------VNPvhagPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQT 216

                        250
                 ....*....|...
gi 528520972 547 PEQYYFCHAAILE 559
Cdd:cd14620  217 DMQYSFIYQALLE 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 314-558 1.04e-53

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: 182.78  E-value: 1.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 314 NQERNRYGDVLCLDQTRVRLKARRNER-SDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDE 392
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 393 GGRRKCGQYWPQEEgGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPS--SAVSLIDFL 470
Cdd:cd14614   92 KRRVKCDHYWPFTE-EPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPTanAAESILQFV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 471 GAVKHQqqwAVQAFGtqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQY 550
Cdd:cd14614  169 QMVRQQ---AVKSKG----------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                 ....*...
gi 528520972 551 YFCHAAIL 558
Cdd:cd14614  236 IFIHQCVQ 243
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 273-559 2.75e-53

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: 182.93  E-value: 2.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 273 MSLAELMAHLNRAQRsgIYLEYEELRREQP-PGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRN-ERSDYINAS-FM 349
Cdd:cd14609    2 MILAYMEDHLRNRDR--LAKEWQALCAYQAePNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 350 DGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYgYIAVVNhRVDNH---A 426
Cdd:cd14609   80 EHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDE--GSSLY-HIYEVN-LVSEHiwcE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 427 HYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKhqqqwavqafgTQWRGHPLgpPMVVHCSAGIG 506
Cdd:cd14609  156 DFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVN-----------KCYRGRSC--PIIVHCSDGAG 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528520972 507 RTGTFCALDICLSQL-QDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14609  223 RTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 290-562 3.32e-53

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: 182.89  E-value: 3.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 290 IYLEYEELRREQPPGTFTCALAAHNQERNRYGDVLCLDQTRVRLKARRNERSDYINASFMDGY--KQKNAYIGTQGPLEK 367
Cdd:cd14599   14 VFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTvgGEEWHYIATQGPLPH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 368 TYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQ--EEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQ 445
Cdd:cd14599   94 TCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 446 VTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRGHplgPPMVVHCSAGIGRTGTFCALDICLSQLQDVG 525
Cdd:cd14599  174 VWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLDSTKNCN---PPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 528520972 526 TLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILEHAQ 562
Cdd:cd14599  251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 342-557 4.93e-53

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: 179.43  E-value: 4.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 342 DYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegGQEVYGYIAVVNHR 421
Cdd:cd14622    1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE--GSVTHGEITIEIKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 422 VDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtQWRGHPLgppmVVHC 501
Cdd:cd14622   79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQ--------QTGNHPI----VVHC 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528520972 502 SAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:cd14622  147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 317-559 5.70e-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: 180.42  E-value: 5.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLK-ARRNERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGR 395
Cdd:cd14602    1 KNRYKDILPYDHSRVELSlITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 396 RKCGQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKH 475
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 476 QQqwavqafgtqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDvGTLNICQTV----RRMRSQRAFSIQTPEQYY 551
Cdd:cd14602  159 YQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKD-GIIPENFSVfsliQEMRTQRPSLVQTKEQYE 224


                 ....*...
gi 528520972 552 FCHAAILE 559
Cdd:cd14602  225 LVYNAVIE 232
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 330-559 1.23e-52

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: 179.06  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 330 RVRLKARRNE-RSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEegg 408
Cdd:cd14631    1 RVILQPVEDDpSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 409 QEVYGYIAVVNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqw 488
Cdd:cd14631   78 TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNP---------- 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528520972 489 rghPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14631  148 ---PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 343-554 3.11e-52

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: 177.23  E-value: 3.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRV 422
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAH-YNQTTLELhnTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQqwavqafGTQwrghplGPPMVVHC 501
Cdd:cd14542   81 KRVGPdFLIRTLKV--TFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQ-------GSE------DVPICVHC 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528520972 502 SAGIGRTGTFCALDICLSQLQDVG---TLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14542  146 SAGCGRTGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 342-559 5.20e-52

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: 177.06  E-value: 5.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 342 DYINASFMD----GYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPqEEGGQEVYGYIAV 417
Cdd:cd14601    1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWP-EPSGSSSYGGFQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 418 VNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrGHPlgPPM 497
Cdd:cd14601   80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRA-----------GKD--EPV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528520972 498 VVHCSAGIGRTGTFCALD--ICLSQL-QDVGTLNIcqtVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14601  147 VVHCSAGIGRTGVLITMEtaMCLIECnQPVYPLDI---VRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 343-555 1.17e-51

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: 175.73  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKN--AYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR-KCGQYWPQEEGGQEVYGYIAVVN 419
Cdd:cd17658    1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 420 HRVDNHAH-YNQTTLELHNTETFEQ-RQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQqwavqafgtqwrghPLGPPM 497
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP--------------PSAGPI 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 498 VVHCSAGIGRTGTFCALDICLSQ--LQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHA 555
Cdd:cd17658  147 VVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 343-559 3.48e-51

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: 174.55  E-value: 3.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASF--MDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWP-QEEGGQEVYGYiavvN 419
Cdd:cd14596    1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMELENY----Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 420 HRVDNH---AHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQqqwavqafgtqwrgHPLGPp 496
Cdd:cd14596   77 LRLENYqalQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKV--------------HNTGP- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528520972 497 MVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14596  142 IVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 317-557 1.83e-50

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: 174.67  E-value: 1.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKARRNER--SDYINASFMDGY-KQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEG 393
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 394 GRrKCGQYWPQEeggQEVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAV 473
Cdd:cd14613  108 NE-KCTEYWPEE---QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 474 KHQQQWAVQAFGtqwrghplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFC 553
Cdd:cd14613  182 EEARQQAEPNCG----------PVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                 ....
gi 528520972 554 HAAI 557
Cdd:cd14613  252 HHVL 255
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 318-554 5.96e-49

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: 169.32  E-value: 5.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 318 NRYGDVLCLDQTRVRLKARRN-ERSDYINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 KCGQYWPQEEGGQEVYGYIAVVnhRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQ 476
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVIT--KLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972 477 QqwavqafgtqwrgHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14616  159 R-------------AHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 317-554 4.14e-48

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: 167.02  E-value: 4.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKARRNER--SDYINASFMDGYK-QKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEG 393
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDslSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 394 GRrKCGQYWPQEEGgqeVYGYIAVVNHRVDNHAHYNQTTLELHNTEtfEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAV 473
Cdd:cd14611   82 NE-KCVLYWPEKRG---IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 474 KHQQQwavqafGTQWRGhplgpPMVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFC 553
Cdd:cd14611  156 EEDRL------ASPGRG-----PVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                 .
gi 528520972 554 H 554
Cdd:cd14611  225 H 225
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 343-554 9.15e-45

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


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 157.18  E-value: 9.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGrRKCGQYWPQEEGGQevYGYIAV--VNH 420
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGT--YGPIQVefVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 421 RVDNHAhyNQTTLELHNTETFEQ--RQVTHFQFLSWPDYG-VPSSAVSLIDFLGAVkhqqqwavqafgTQWRGHPLGPPM 497
Cdd:cd14556   78 TIDEDV--ISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEV------------EKWQEQSGEGPI 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528520972 498 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14556  144 VVHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 343-559 4.09e-39

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: 142.81  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMD---GYKQKNaYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWPQ--EEGGQEVYGYIAV 417
Cdd:cd14598    1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 418 VNHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQWAVQAFGTQwrgHPlGPPM 497
Cdd:cd14598   80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPK---SP-NPPV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972 498 VVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14598  156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 445-559 1.18e-38

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   445 QVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQD- 523
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN-----------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAe 69

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 528520972   524 VGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:smart00012  70 AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
445-559 1.18e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 137.10  E-value: 1.18e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   445 QVTHFQFLSWPDYGVPSSAVSLIDFLGAVKHQQQwavqafgtqwrGHPLGPPMVVHCSAGIGRTGTFCALDICLSQLQD- 523
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLN-----------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAe 69

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 528520972   524 VGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:smart00404  70 AGEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 343-559 5.83e-35

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: 130.91  E-value: 5.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGgrRKCGQYWPQEEGGqeVYGYIAVVNHRV 422
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTSC--CYGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQ--RQVTHFQFLSWPDY-GVPSSAVSLidfLGAVKHQQQWAVQAFGTQWRghplgppMVV 499
Cdd:cd14634   77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSI---LKVVRRLEKWQEQYDGREGR-------TVV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 500 HCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14634  147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
317-550 8.84e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.52  E-value: 8.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 317 RNRYGDVLCLDQTRVRLKARrnersdYINASFMDGyKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR 396
Cdd:COG5599   45 LNRFRDIQPYKETALRANLG------YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 397 --KCGQYWPQeeggQEVYGYIAVVNHRVDNHahYNQTTLELHnteTF---------EQRQVTHFQFLSWPDYGVPSSAVs 465
Cdd:COG5599  118 kvKMPVYFRQ----DGEYGKYEVSSELTESI--QLRDGIEAR---TYvltikgtgqKKIEIPVLHVKNWPDHGAISAEA- 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 466 LIDFLGAVKHQQQWavqafgtqwRGHPLGPPmVVHCSAGIGRTGTFCALdICLSQLQDVG---TLNICQTVRRMRSQRAF 542
Cdd:COG5599  188 LKNLADLIDKKEKI---------KDPDKLLP-VVHCRAGVGRTGTLIAC-LALSKSINALvqiTLSVEEIVIDMRTSRNG 256


                 ....*....
gi 528520972 543 SI-QTPEQY 550
Cdd:COG5599  257 GMvQTSEQL 265
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 343-559 5.45e-31

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: 119.79  E-value: 5.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGgrRKCGQYWPqeEGGQEVYGYIAVVNHRV 422
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWP--ENGVHRHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQ--RQVTHFQFLSWPDYgvPSSAVSLIDFLGAVKHQQQWAVQAFGTQWRghplgppMVVH 500
Cdd:cd14635   77 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEYNGGEGR-------TVVH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 501 CSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14635  148 CLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 288-557 6.37e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 122.38  E-value: 6.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 288 SGIYLEYEELRREQPPGtftcALAAHNQERNRYGD-VLCLDQTRV---RLKARRNERsdYINASFMDGYKQKNAYIGTQG 363
Cdd:PHA02740  25 SCIIKEYRAIVPEHEDE----ANKACAQAENKAKDeNLALHITRLlhrRIKLFNDEK--VLDARFVDGYDFEQKFICIIN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 364 PLEKTYGDFWRMVWEQNVLVIVMTTRTDEggrRKC-GQYWPQEEGGQEVYGYIAVVNHRVDNHAHYNQTTLELhnTETFE 442
Cdd:PHA02740  99 LCEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSL--TDKFG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 443 Q-RQVTHFQFLSWPDYGVPSSAVSLIDFLGAVKH-----QQQWAVQAFGtqwrghplgpPMVVHCSAGIGRTGTFCALDI 516
Cdd:PHA02740 174 QaQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlEKHKADGKIA----------PIIIDCIDGISSSAVFCVFDI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 528520972 517 CLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAI 557
Cdd:PHA02740 244 CATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 343-552 2.91e-30

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: 117.42  E-value: 2.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGrrKCGQYWPQEEGGQEVYGY----IAVV 418
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFkvtlSGED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 419 NHRVDNHAHYNQTTLELHNTETFEQRQVTHFQFLSWPDygvPSSavSLIDFLGAVKHQQQWAVQAFGtqwrghplgpPMV 498
Cdd:cd14550   79 HSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCS--PIHTVFELINTVQEWAQQRDG----------PIV 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528520972 499 VHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYF 552
Cdd:cd14550  144 VHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 81-231 1.07e-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: 111.62  E-value: 1.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972    81 ELLSGKFTVLGVR--DPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAV--ESFETQRNGLVFIYDMAGSNYTNFEL 156
Cdd:smart00516   1 ELELLKAYIPGGRgyDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILqeEKKTGGIEGFTVIFDLKGLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972   157 DLSKKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVKMA---DLRQHLPRDCLPEHLGGCLP 231
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDskeELLEYIDKEQLPEELGGTLD 158
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 343-559 1.54e-27

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: 110.11  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGgrRKCGQYWPQEegGQEVYGYIAVVNHRV 422
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEE--GMLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHNTETFEQ--RQVTHFQFLSWPDY-GVPSSAVSLIDFLGAVKHQQQWAVQAFGTqwrghplgppMVV 499
Cdd:cd14636   77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGR----------TII 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 500 HCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14636  147 HCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 83-228 2.64e-27

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: 107.81  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  83 LSGKFTVLGVRDPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAVESFETQRNGLVFIYDMAGSNYTNF-ELDLSKK 161
Cdd:cd00170    7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLKGFSLSNLsDLSLLKK 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528520972 162 ILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK--MADLRQHLPRDCLPEHLGG 228
Cdd:cd00170   87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGG 155
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 343-559 2.38e-26

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: 106.53  E-value: 2.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRR-KCGQYWPqeEGGQEVYGYIAVvnHR 421
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP--EPGLQQYGPMEV--EF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 422 VDNHAHYNQTT--LELHNTETFEQRQ--VTHFQFLSWPDY-GVPSSAVSLIDFLGAVkhqQQWavQAFGTQWRghplgpp 496
Cdd:cd14637   77 VSGSADEDIVTrlFRVQNITRLQEGHlmVRHFQFLRWSAYrDTPDSKKAFLHLLASV---EKW--QRESGEGR------- 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528520972 497 MVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAILE 559
Cdd:cd14637  145 TVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
CRAL_TRIO pfam00650
CRAL/TRIO domain;
84-228 7.33e-25

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 100.79  E-value: 7.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   84 SGKFTVLGvRDPSGASIALYTAKLHHPSKTGNHVVLQALFYLLDRAV-ESFETQRNGLVFIYDMAGSNYTNFE---LDLS 159
Cdd:pfam00650   1 GGKVYLHG-RDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALlLMPEGQVEGLTVIIDLKGLSLSNMDwwsISLL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972  160 KKILNLLKGAFPARLKKVLIVGAPVWFRVPYNLLSLLLKEKLRERVQMVK---MADLRQHLPRDCLPEHLGG 228
Cdd:pfam00650  80 KKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsnEEELEKYIPPEQLPKEYGG 151
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 343-558 3.41e-24

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: 100.45  E-value: 3.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCgQYWPQEEGGQEVYGYiAVVNHRV 422
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETF-KVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHN-----TETFEQRQVTHFQFLSWPDygvPSSAVS-LIDFLGAVKHQqqwAVQAFGtqwrghplgpP 496
Cdd:cd17669   79 EHKCLSNEEKLIIQDfileaTQDDYVLEVRHFQCPKWPN---PDSPISkTFELISIIKEE---AANRDG----------P 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972 497 MVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAIL 558
Cdd:cd17669  143 MIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 343-558 9.87e-23

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: 96.29  E-value: 9.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 343 YINASFMDGYKQKNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTrTDEGGRRKCGQYWPQEEGGQEVYGYIAVVNHRv 422
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQGLAEDEFVYWPSREESMNCEAFTVTLISK- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 423 DNHAHYNQTTLELHN-----TETFEQRQVTHFQFLSWPDYGVP-SSAVSLIDFLgavkhqQQWAVQAFGtqwrghplgpP 496
Cdd:cd17670   79 DRLCLSNEEQIIIHDfileaTQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI------KEEALTRDG----------P 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528520972 497 MVVHCSAGIGRTGTFCALDICLSQLQDVGTLNICQTVRRMRSQRAFSIQTPEQYYFCHAAIL 558
Cdd:cd17670  143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 493-554 4.05e-11

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: 60.06  E-value: 4.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528520972 493 LGPPMVVHCSAGIGRTGTFCALDICLSQLQDVGtlnicQTVRRMRSQRAFSI-QTPEQYYFCH 554
Cdd:cd14494   55 PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAE-----EAVRIVRLIRPGGIpQTIEQLDFLI 112
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 439-554 4.33e-08

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: 53.89  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 439 ETFEQRQVTHFQFlSWPDYGVPSSA-----VSLIDFlgAVKHQQQWAVqafgtqwrghplgppmvvHCSAGIGRTGTF-- 511
Cdd:cd14506   70 EAFMRAGIYFYNF-GWKDYGVPSLTtildiVKVMAF--ALQEGGKVAV------------------HCHAGLGRTGVLia 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528520972 512 CALdiclsqlqdVGTLNIC--QTVRRMRSQRAFSIQTPEQYYFCH 554
Cdd:cd14506  129 CYL---------VYALRMSadQAIRLVRSKRPNSIQTRGQVLCVR 164
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 355-550 2.83e-07

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: 51.63  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 355 KNAYIGTQGPLEKTYGDFWRMVWEQNVLVIVMTTRTDEGGRRKCGQYWpqeeGGQEVYGYIAVVNHRVDNHAHYNQTTLE 434
Cdd:cd14559   28 KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTVKSKKTGKDELVDGLKAD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 435 LHNTETfEQRQVTH----FQFLSWPDYGVPSSAV--SLIDFLGAVKHQQQWAVQAFGTQWRGHPLGPPMVVHCSAGIGRT 508
Cdd:cd14559  104 MYNLKI-TDGNKTItipvVHVTNWPDHTAISSEGlkELADLVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRT 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528520972 509 GTFCAlDICLSQLQDvgTLNICQTVRRMRSQR-AFSIQTPEQY 550
Cdd:cd14559  183 GQLAA-AMELNKSPN--NLSVEDIVSDMRTSRnGKMVQKDEQL 222
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 97-233 2.84e-07

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: 50.02  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972   97 GASIALYTAKLHHPSKTGNHVVLQALFYLLDRAVESFETQrnGLVFIYDMAGSNYTNFE-LDLSKKILNLLKGAFPARLK 175
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGK--PFVVVVDHTGVTSENFPsLSFLKKAYDLLPRAFKKNLK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972  176 KVLIVGAPVWFR--VPYNLLSLLLKEKLRERVQMVKMADLRQHLPRDCLPEHLGGCLPLD 233
Cdd:pfam13716  79 AVYVVHPSTFLRtfLKTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYD 138
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
11-59 3.95e-07

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 46.77  E-value: 3.95e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 528520972    11 EQATKQFLEEINKWTSQHgVSPLSWDVAVKFLMARKFDVLRAIELFHSY 59
Cdd:smart01100   1 EEALEELRELLEKHPDLL-PPRLDDAFLLRFLRARKFDVEKAKEMLEKY 48
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 498-555 3.23e-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: 44.56  E-value: 3.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528520972 498 VVHCSAGIGRTGTFCALdiCLSQLQDvgTLNICQTVRRMRSQRAFSIQTPEQYYFCHA 555
Cdd:cd14505  110 LIHCKGGLGRTGLIAAC--LLLELGD--TLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
431-552 3.90e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.81  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 431 TTLELHNTETFEQRQVTHFQFlSWPDYGVPSSAvSLIDFLGAVKHQQQwavqafgtqwRGHPLgppmVVHCSAGIGRTGT 510
Cdd:COG2453   33 TEEEELLLGLLEEAGLEYLHL-PIPDFGAPDDE-QLQEAVDFIDEALR----------EGKKV----LVHCRGGIGRTGT 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528520972 511 FCAldiCLSQLQDVGTLNICQTVRRMRSQrafSIQTPEQYYF 552
Cdd:COG2453   97 VAA---AYLVLLGLSAEEALARVRAARPG---AVETPAQRAF 132
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 451-549 2.82e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528520972 451 FLSWPDYGVPSsaVSLID-FLGAVKHQQQwavqafgtqwrghpLGPPMVVHCSAGIGRTGTFCAldiCLsqLQDVGTLNI 529
Cdd:cd14504   54 HIPIEDYTPPT--LEQIDeFLDIVEEANA--------------KNEAVLVHCLAGKGRTGTMLA---CY--LVKTGKISA 112

                         90       100
                 ....*....|....*....|
gi 528520972 530 CQTVRRMRSQRAFSIQTPEQ 549
Cdd:cd14504  113 VDAINEIRRIRPGSIETSEQ 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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