NCBI Conserved Domain Search

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

134-221

9.84e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 9.84e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  134 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 208
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                           90
                   ....*....|...
gi 2462566564  209 GINSSRETRNATT 221
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

45-132

1.20e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.27 E-value: 1.20e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   45 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 120
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 2462566564  121 VNSSVGTVTTAT 132
Cdd:cd00063     81 GESPPSESVTVT 92

fn3

Fibronectin type III domain;

225-292

4.98e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 4.98e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566564  225 PVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQC----TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSV 292
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

Name

Accession

Description

Interval

E-value

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

859-1091

4.18e-162

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 479.00 E-value: 4.18e-162

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 1018
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462566564 1019 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14619    161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

830-1089

1.13e-114

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 355.81 E-value: 1.13e-114

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   830 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 908
Cdd:smart00194    1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   909 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSV 987
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   988 RQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMR 1067
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 2462566564  1068 ESRPLMVQTEAQYVFLHQCILR 1089
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

855-1088

8.71e-106

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 331.13 E-value: 8.71e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 1012
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564 1013 MLRQWlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:pfam00102  159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PHA02742

protein tyrosine phosphatase; Provisional

854-1090

6.87e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.93 E-value: 6.87e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:PHA02742    51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 1012
Cdd:PHA02742   129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1013 MLRQwLDQTME---------GGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 1082
Cdd:PHA02742   209 AVRE-ADLKADvdikgenivKEPPIlVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                   ....*...
gi 2462566564 1083 LHQCILRF 1090
Cdd:PHA02742   288 CYFIVLIF 295

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

854-1096

4.54e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 147.16 E-value: 4.54e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:COG5599     41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAG--RVKCEHYWPLDSQPCTHgHLRVTLVGEEV-MENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSpDTLLA 1009
Cdd:COG5599    113 EISkpKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISA-EALKN 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1010 FWRMLRQWLD-QTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLgPFSF---VRKMRESR-PLMVQTEAQYVFLh 1084
Cdd:COG5599    191 LADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQI-TLSVeeiVIDMRTSRnGGMVQTSEQLDVL- 268

                          250
                   ....*....|..
gi 2462566564 1085 qcILRFLQQSAQ 1096
Cdd:COG5599    269 --VKLAEQQIRP 278

FN3

Fibronectin type 3 domain [General function prediction only];

261-698

3.32e-12

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 70.80 E-value: 3.32e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  261 TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNS----SVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPD 336
Cdd:COG3401     84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTattaTAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  337 GPDPQNSTYGVEYTGDGGRAGTRSTAHT-NITVDRLEPGCLYVFSVWVGKNGINSSRETR----NATTAPNPVRNLHMET 411
Cdd:COG3401    164 AGAGVVVSPDTSATAAVATTSLTVTSTTlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATA 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  412 QTNSSIALCWEVPDGPYPQdyTYWVEYTGDGGGTETR--NTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSIS-- 487
Cdd:COG3401    244 DTPGSVTLSWDPVTESDAT--GYRVYRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSvt 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  488 ---TVPNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAER 564
Cdd:COG3401    322 tdlTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVD 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  565 ---------NEVRGYNSTLTAATAPNEVTDLqNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRGQDPQANWVN 635
Cdd:COG3401    402 aagnesapsEEVSATTASAASGESLTASVDA-VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566564  636 QTSRTNETWYKVEALEPGTLYNFTVWAE-RNDVASSTQSLYPDTVTITSCVSTSAGYGVNLIWS 698
Cdd:COG3401    481 TTDTTTANLSVTTGSLVGGSGASSVTNSvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

401-479

8.53e-11

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 59.43 E-value: 8.53e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  401 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 476
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ...
gi 2462566564  477 ARG 479
Cdd:cd00063     81 GES 83

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

401-473

5.82e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.85 E-value: 5.82e-10

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462566564   401 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 473
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

134-221

9.84e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 9.84e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  134 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 208
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                           90
                   ....*....|...
gi 2462566564  209 GINSSRETRNATT 221
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

45-132

1.20e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.27 E-value: 1.20e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   45 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 120
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 2462566564  121 VNSSVGTVTTAT 132
Cdd:cd00063     81 GESPPSESVTVT 92

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

134-205

8.36e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.99 E-value: 8.36e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566564   134 PNPVRNLRVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDGLEPGCLYAFSMWV 205
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76

fn3

Fibronectin type III domain;

582-660

2.85e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.25 E-value: 2.85e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564  582 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 660
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73

fn3

Fibronectin type III domain;

225-292

4.98e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 4.98e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566564  225 PVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQC----TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSV 292
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

45-123

1.75e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.14 E-value: 1.75e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564    45 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 120
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 2462566564   121 VNS 123
Cdd:smart00060   81 GEG 83

fn3

Fibronectin type III domain;

43-114

7.70e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.40 E-value: 7.70e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564   43 PAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 114
Cdd:pfam00041    1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73

fn3

Fibronectin type III domain;

136-216

3.37e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 40.48 E-value: 3.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  136 PVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDGLEPGCLYAFSMwVGKNGIN 211
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                   ....*
gi 2462566564  212 SSRET 216
Cdd:pfam00041   81 EGPPS 85

Name

Accession

Description

Interval

E-value

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

859-1091

4.18e-162

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 479.00 E-value: 4.18e-162

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 1018
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462566564 1019 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14619    161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

860-1085

3.86e-141

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: 424.07 E-value: 3.86e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  860 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 939
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  940 CEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLD 1019
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVR--SVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564 1020 QtmEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14548    159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

830-1089

1.13e-114

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 355.81 E-value: 1.13e-114

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   830 GFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQEFIATQGPLP 908
Cdd:smart00194    1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   909 QTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSV 987
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   988 RQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMR 1067
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 2462566564  1068 ESRPLMVQTEAQYVFLHQCILR 1089
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

855-1088

8.71e-106

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 331.13 E-value: 8.71e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTG--DPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 AGRVKCEHYWPLDS-QPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 1012
Cdd:pfam00102   79 KGREKCAQYWPEEEgESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564 1013 MLRQWlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:pfam00102  159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

859-1088

5.04e-100

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: 315.73 E-value: 5.04e-100

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 1018
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1019 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14618    161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

859-1088

1.04e-95

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: 304.05 E-value: 1.04e-95

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKpIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWL 1018
Cdd:cd14615     80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1019 DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14615    159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

885-1085

1.80e-90

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: 288.80 E-value: 1.80e-90

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLVGE 963
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRTGTLIA 1043
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKP--NGPIVVHCSAGVGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462566564 1044 LDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd00047    159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

859-1085

3.72e-88

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: 283.73 E-value: 3.72e-88

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQvEEQKTLS--VRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 1016
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICS-EEQLDAPrlVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1017 WLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14617    160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

855-1088

8.18e-87

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: 280.44 E-value: 8.18e-87

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 AGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRML 1014
Cdd:cd14553     83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566564 1015 RQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14553    162 KAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALL 233

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

855-1088

2.49e-86

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: 279.08 E-value: 2.49e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 AGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEqkTLSVRQFHYQAWPDHGVPS--SPDTLLAFWR 1012
Cdd:cd14614     92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE--VQDVMHFNYTAWPDHGVPTanAAESILQFVQ 169

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564 1013 MLRQWLDQTMegGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14614    170 MVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

830-1084

5.10e-79

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: 260.37 E-value: 5.10e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  830 GFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQ 909
Cdd:cd14543      4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  910 TVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVR 988
Cdd:cd14543     84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSlRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  989 QFHYQAWPDHGVPSSPDTLLAFWRMLRQ---WLDQTM-------EGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLL 1057
Cdd:cd14543    164 HFQFTSWPDFGVPSSAAALLDFLGEVRQqqaLAVKAMgdrwkghPPGPPIvVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243

                          250       260
                   ....*....|....*....|....*..
gi 2462566564 1058 GPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:cd14543    244 NVMQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

885-1084

2.34e-78

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: 255.74 E-value: 2.34e-78

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 964
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLS------VRQFHYQAWPDHGVPSSPDTLLAFWRmlRQWLDQTMEGGPPIVHCSAGVGRT 1038
Cdd:cd14549     80 VLATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSFVR--KSSAANPPGAGPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462566564 1039 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:cd14549    158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

815-1088

3.67e-75

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: 249.95 E-value: 3.67e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  815 DFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 894
Cdd:cd14626      2 DLADNIERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  895 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVREL 974
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTE-TYGMIQVTLLDTVELATYSVRTF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  975 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSE 1054
Cdd:cd14626    160 ALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKAC--NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462566564 1055 GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

859-1085

9.00e-74

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: 243.66 E-value: 9.00e-74

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV 938
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  939 KCEHYWPLDSQPCT-HGHLRVTLVGEEVMENWTVRElllLQVEEQ-KTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 1016
Cdd:cd14616     81 RCHQYWPEDNKPVTvFGDIVITKLMEDVQIDWTIRD---LKIERHgDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1017 wlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14616    158 --SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

811-1088

1.62e-70

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

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 237.32 E-value: 1.62e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  811 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 890
Cdd:cd14624      4 IPILELADHIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  891 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWT 970
Cdd:cd14624     83 IDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTE-TYGLIQVTLLDTVELATYC 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  971 VRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQ 1050
Cdd:cd14624    162 VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTC--NPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462566564 1051 LQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14624    240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

854-1088

1.98e-70

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: 234.92 E-value: 1.98e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRM 1013
Cdd:cd14630     82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462566564 1014 LRqWLDQTmEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14630    160 VK-FLNPP-DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

855-1092

8.79e-70

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: 233.89 E-value: 8.79e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLKPI-HEEPGSDYINASF-MPGLWSPQE------FIATQGPLPQTVGDFWRLVWEQQSHTL 926
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYiRNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  927 VMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTL-SVRQFHYQAWPDHGVPSSPD 1005
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIrEIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1006 TLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYVF 1082
Cdd:cd14544    161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTEAQYKF 240

                          250
                   ....*....|
gi 2462566564 1083 LHQCILRFLQ 1092
Cdd:cd14544    241 IYVAVAQYIE 250

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

850-1088

1.69e-69

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: 232.41 E-value: 1.69e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  850 ASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVML 929
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  930 TNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLA 1009
Cdd:cd14554     81 TKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1010 FWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14554    160 FIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

846-1087

2.63e-69

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: 233.18 E-value: 2.63e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  846 SQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 925
Cdd:cd14603     21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  926 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEE-VMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSP 1004
Cdd:cd14603    101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKVTFQKESR--SVSHFQYMAWPDHGIPDSP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1005 DTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYV 1081
Cdd:cd14603    179 DCMLAMIELARRL--QGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIfdvVLEMRKQRPAAVQTEEQYE 256


                   ....*.
gi 2462566564 1082 FLHQCI 1087
Cdd:cd14603    257 FLYHTV 262

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

885-1085

9.41e-69

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: 9.41e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFM-PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGE 963
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EV--MENWTVRELLLlQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTL 1041
Cdd:cd18533     81 EEndDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462566564 1042 IALDVLLRQLQSEGLLGP---------FSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd18533    160 IALDSLLDELKRGLSDSQdledsedpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

811-1088

1.37e-68

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

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 231.52 E-value: 1.37e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  811 IPAEDFADHVRKNERDSNCGFADEYQQLSlVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 890
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  891 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWT 970
Cdd:cd14625     83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATFC 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  971 VRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQ 1050
Cdd:cd14625    162 VRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTC--NPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462566564 1051 LQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14625    240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

815-1088

1.80e-68

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: 231.08 E-value: 1.80e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  815 DFADHVRKNERDSNCGFADEYQQLsLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGL 894
Cdd:cd14633      1 DLLQHITQMKCAEGYGFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  895 WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEEVMENWTVREL 974
Cdd:cd14633     80 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  975 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSE 1054
Cdd:cd14633    158 AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAERE 235

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462566564 1055 GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14633    236 GVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

811-1088

3.26e-68

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: 231.07 E-value: 3.26e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  811 IPAEDFADHVRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASF 890
Cdd:cd14621      8 LPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASF 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  891 MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPldSQPC-THGHLRVTLVGEEVMENW 969
Cdd:cd14621     88 INGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCwTYGNIRVSVEDVTVLVDY 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  970 TVRELLLLQV----EEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRTGTLIALD 1045
Cdd:cd14621    166 TVRKFCIQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQY--AGAIVVHCSAGVGRTGTFIVID 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462566564 1046 VLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14621    244 AMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

854-1091

8.63e-68

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: 227.41 E-value: 8.63e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPIHeepgsDYINASFMPGLWSPQEF--IATQGPLPQTVGDFWRLVWEQQSHTLVMLTN 931
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  932 CMEAGRVKCEHYWP--LDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLA 1009
Cdd:cd14597     77 EVEGGKIKCQRYWPeiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1010 FWRMLRqwldQTMEGGPPIVHCSAGVGRTGTLIALDVLLrQLQSEGLLGPFS-FVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14597    157 FISYMR----HIHKSGPIITHCSAGIGRSGTLICIDVVL-GLISKDLDFDISdIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                   ...
gi 2462566564 1089 RFL 1091
Cdd:cd14597    232 YVL 234

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

850-1089

1.13e-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: 228.58 E-value: 1.13e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  850 ASASENNAKNRYRNVLPYDWSRVPLkpiheEPGSDYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHT 925
Cdd:cd14600     35 AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  926 LVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPD 1005
Cdd:cd14600    110 IVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1006 TLLAFWRMLRQwldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14600    190 DFLEFVNYVRS---KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCE 266


                   ....
gi 2462566564 1086 CILR 1089
Cdd:cd14600    267 AILR 270

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

859-1085

5.96e-66

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: 221.89 E-value: 5.96e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  859 NRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAg 936
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRG-YDGEEkaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  937 RVKCEHYWPlDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKtlSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 1016
Cdd:cd14547     79 KEKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKR--YLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1017 WLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14547    156 ARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

861-1088

1.18e-65

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 221.35 E-value: 1.18e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  861 YRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKC 940
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  941 EHYWPldSQPC-THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVR---QFHYQAWPDHGVPSSPDTLLAFWRMLRQ 1016
Cdd:cd14620     81 YQYWP--DQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566564 1017 WldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14620    159 V--NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

831-1088

2.69e-65

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: 222.22 E-value: 2.69e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  831 FADEYQQlslVGHSQSQMVASAS-----ENNAKNRYRNVLPYDWSRVPLKPI--HEEPGSDYINASFMPGLWSPQEFIAT 903
Cdd:cd17667      1 FSEDFEE---VQRCTADMNITAEhsnhpDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  904 QGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEEVMENWTVRELLLLQVEEQK 983
Cdd:cd17667     78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  984 TL-----------SVRQFHYQAWPDHGVPSSPDTLLAFWRmlRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQ 1052
Cdd:cd17667    157 GQkgnpkgrqnerTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462566564 1053 SEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd17667    235 DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

885-1091

5.12e-64

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: 215.70 E-value: 5.12e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP--LDSQPCTHGHLRVTL 960
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  961 VGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDqtmeGGPPIVHCSAGVGRTGT 1040
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHN----SGPIVVHCSAGIGRTGV 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14538    157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

884-1089

5.31e-64

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: 216.04 E-value: 5.31e-64

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  884 DYINASF----MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 959
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  960 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEggPPIVHCSAGVGRTG 1039
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--PTVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1040 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILR 1089
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

858-1082

7.19e-63

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: 213.41 E-value: 7.19e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  858 KNRYRNVLPYDWSRVPLKpIHEEpGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 937
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVK-LKQG-DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  938 VKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRML 1014
Cdd:cd14545     79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566564 1015 RQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGpfSFVRK----MRESRPLMVQTEAQYVF 1082
Cdd:cd14545    159 RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSS--VDVKKvlleMRKYRMGLIQTPDQLRF 228

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

810-1091

2.27e-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: 214.60 E-value: 2.27e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  810 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 884
Cdd:cd14628      2 EVPARNLYAYIQKLTQietgENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 964
Cdd:cd14628     82 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14628    161 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462566564 1045 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14628    241 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

871-1088

2.69e-62

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: 211.42 E-value: 2.69e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  871 RVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQp 950
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  951 cTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwLDQTMEGGPPIVH 1030
Cdd:cd14631     80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566564 1031 CSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

885-1088

3.75e-62

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: 210.54 E-value: 3.75e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 964
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwLDQTMEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14555     79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462566564 1045 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14555    157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

854-1092

1.17e-61

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: 211.03 E-value: 1.17e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLkpiHE----EPGSDYINASF-MPGLWS-------PQEFIATQGPLPQTVGDFWRLVWEQ 921
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVL---HDgdpnEPVSDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  922 QSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKT-LSVRQFHYQAWPDHGV 1000
Cdd:cd14605     78 NSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1001 PSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL---LGPFSFVRKMRESRPLMVQTE 1077
Cdd:cd14605    158 PSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTE 237

                          250
                   ....*....|....*
gi 2462566564 1078 AQYVFLHQCILRFLQ 1092
Cdd:cd14605    238 AQYRFIYMAVQHYIE 252

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

810-1091

1.26e-61

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: 212.29 E-value: 1.26e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  810 DIPAEDFADHVRKNER----DSNCGFADEYQQLS-LVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 884
Cdd:cd14627      3 EVPARNLYSYIQKLAQvevgEHVTGMELEFKRLAnSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 964
Cdd:cd14627     83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14627    162 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462566564 1045 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14627    242 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

854-1093

1.43e-61

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: 212.49 E-value: 1.43e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAGRVKCEHYWPL-DSQPCTHGHLRVTLVGEEVMENWTVRELLllqVE-EQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW 1011
Cdd:cd14604    136 EMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTDYFIRTLL---LEfQNETRRLYQFHYVNWPDHDVPSSFDSILDMI 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1012 RMLRQWldQTMEGGPPIVHCSAGVGRTGTLIALDV---LLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14604    213 SLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIA 290


                   ....*
gi 2462566564 1089 RFLQQ 1093
Cdd:cd14604    291 QLFEK 295

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

810-1091

4.41e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 210.74 E-value: 4.41e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  810 DIPAEDFADHVRKNER----DSNCGFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSD 884
Cdd:cd14629      3 EVPARNLYAHIQKLTQvppgESVTAMELEFKLLaNSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDsQPCTHGHLRVTLVGEE 964
Cdd:cd14629     83 YINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14629    162 NMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITL 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462566564 1045 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14629    242 SIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

858-1088

5.61e-61

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: 208.16 E-value: 5.61e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  858 KNRYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR 937
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  938 VKCEHYWP-LDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTlsVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQ 1016
Cdd:cd14602     81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRT--IYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564 1017 WldQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQsEGLL----GPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14602    159 Y--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

885-1085

2.03e-60

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: 205.35 E-value: 2.03e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC-THGHLRVTLVGE 963
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVM-ENWTVRELLLLQVEEQKTlsVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLI 1042
Cdd:cd14542     81 KRVgPDFLIRTLKVTFQKESRT--VYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462566564 1043 ALDVLLRQLQSEGL---LGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14542    157 AIDYVWNLLKTGKIpeeFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

854-1092

3.26e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.

Pssm-ID: 350454 [Multi-domain] Cd Length: 266 Bit Score: 207.43 E-value: 3.26e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPIHEE-PGSDYINASFMPG-LWSPQE----FIATQGPLPQTVGDFWRLVWEQQSHTLV 927
Cdd:cd14606     17 ENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGPDEnaktYIASQGCLEATVNDFWQMAWQENSRVIV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  928 MLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSPDT 1006
Cdd:cd14606     97 MTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNgELIREIWHYQYLSWPDHGVPSEPGG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1007 LLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF---VRKMRESRPLMVQTEAQYVFL 1083
Cdd:cd14606    177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIqktIQMVRAQRSGMVQTEAQYKFI 256


                   ....*....
gi 2462566564 1084 HQCILRFLQ 1092
Cdd:cd14606    257 YVAIAQFIE 265

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

885-1085

4.79e-60

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.

Pssm-ID: 350405 [Multi-domain] Cd Length: 201 Bit Score: 204.29 E-value: 4.79e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQPCTHGHLRVTLVGE 963
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVMENWTVRELLLLQVEEQKT-LSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWldQTMEGGPPIVHCSAGVGRTGTLI 1042
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF--NNFFSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462566564 1043 ALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

885-1085

1.10e-59

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: 203.22 E-value: 1.10e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 964
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQV----EEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLdqTMEGGPPIVHCSAGVGRTGT 1040
Cdd:cd14551     80 VLVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRTGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14551    158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

885-1088

2.42e-59

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: 202.59 E-value: 2.42e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 964
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14632     79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIVL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462566564 1045 DVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14632    157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

885-1087

3.16e-57

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: 196.34 E-value: 3.16e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGEE 964
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPI-VHCSAGVGRTGTLIA 1043
Cdd:cd14552     80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS--GNHPItVHCSAGAGRTGTFCA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462566564 1044 LDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 1087
Cdd:cd14552    158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

884-1090

3.87e-57

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: 196.38 E-value: 3.87e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  884 DYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpCTHGHLRVTLVGE 963
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmeGGPPI-VHCSAGVGRTGTLI 1042
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--GNHPIvVHCSAGAGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462566564 1043 ALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRF 1090
Cdd:cd14622    158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

860-1087

4.98e-57

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: 196.80 E-value: 4.98e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  860 RYRNVLPYDWSRVPLKPIHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVK 939
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  940 CEHYWPLDSQpCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlD 1019
Cdd:cd14623     81 CAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK--Q 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1020 QTMEGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 1087
Cdd:cd14623    158 QQQSGNHPItVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

885-1088

3.44e-56

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: 193.66 E-value: 3.44e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPcTHGHLRVTLVGEE 964
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVE----EQKTLS----VRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVG 1036
Cdd:cd17668     80 VLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462566564 1037 RTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

831-1082

5.24e-56

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: 195.63 E-value: 5.24e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  831 FADEYQQLSlvgHSQSQM---VASASENNAKNRYRNVLPYDWSRVPLkpiHEEpGSDYINASFMPGLWSPQEFIATQGPL 907
Cdd:cd14608      1 WAAIYQDIR---HEASDFpcrVAKLPKNKNRNRYRDVSPFDHSRIKL---HQE-DNDYINASLIKMEEAQRSYILTQGPL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  908 PQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQP---CTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKT 984
Cdd:cd14608     74 PNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  985 LSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALD---VLLRQLQSEGLLGPFS 1061
Cdd:cd14608    154 REILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKK 233

                          250       260
                   ....*....|....*....|.
gi 2462566564 1062 FVRKMRESRPLMVQTEAQYVF 1082
Cdd:cd14608    234 VLLEMRKFRMGLIQTADQLRF 254

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

885-1084

2.42e-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: 187.99 E-value: 2.42e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQpcTHGHLRVTLVGEE 964
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGG----PPIVHCSAGVGRTGT 1040
Cdd:cd14558     79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:cd14558    159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

843-1087

3.34e-54

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: 189.79 E-value: 3.34e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  843 HSQSQMVASASENNAKNRYRNVLPYDWSRVPLkpihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQ 922
Cdd:cd14607     12 HDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  923 SHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHG 999
Cdd:cd14607     88 TKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsfKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFG 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1000 VPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEgllGPFSFVRK-----MRESRPLMV 1074
Cdd:cd14607    168 VPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKK---DPDSVDIKqvlldMRKYRMGLI 244

                          250
                   ....*....|...
gi 2462566564 1075 QTEAQYVFLHQCI 1087
Cdd:cd14607    245 QTPDQLRFSYMAV 257

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

885-1092

1.12e-53

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: 186.49 E-value: 1.12e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASF--MPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 961
Cdd:cd14596      1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  962 GEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRqwldQTMEGGPPIVHCSAGVGRTGTL 1041
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR----KVHNTGPIVVHCSAGIGRAGVL 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462566564 1042 IALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 1092
Cdd:cd14596    157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

884-1093

9.14e-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: 181.30 E-value: 9.14e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  884 DYINASFM----PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHLRVT 959
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  960 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEggPPIVHCSAGVGRTG 1039
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE--PVVVHCSAGIGRTG 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462566564 1040 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQ 1093
Cdd:cd14601    159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

818-1082

5.07e-51

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: 181.79 E-value: 5.07e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  818 DHVRKNERdsncgFADEYQQL-SLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS-FMPGLW 895
Cdd:cd14610     11 DHLKNKNR-----LEKEWEALcAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  896 SPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MENWTVREL 974
Cdd:cd14610     86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIY-EVNLVSEHIwCEDFLVRSF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  975 LLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFwrmlRQWLDQTMEGG--PPIVHCSAGVGRTGTLIALDVLLRQL- 1051
Cdd:cd14610    165 YLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDF----RRKVNKCYRGRscPIIVHCSDGAGRSGTYILIDMVLNKMa 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462566564 1052 QSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 1082
Cdd:cd14610    241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 271

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

818-1082

1.26e-50

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: 180.62 E-value: 1.26e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  818 DHVRKNERdsncgFADEYQQLSLVGHSQSQMVASASENN-AKNRYRNVLPYDWSRVPLKPIHEEPGSDYINAS------- 889
Cdd:cd14609      9 DHLRNRDR-----LAKEWQALCAYQAEPNTCSTAQGEANvKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdp 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  890 FMPGlwspqeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCTHGHlRVTLVGEEV-MEN 968
Cdd:cd14609     84 RMPA------YIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIY-EVNLVSEHIwCED 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  969 WTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFwrmlRQWLDQTMEGG--PPIVHCSAGVGRTGTLIALDV 1046
Cdd:cd14609    157 FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDF----RRKVNKCYRGRscPIIVHCSDGAGRTGTYILIDM 232

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462566564 1047 LLRQLqSEGL--LGPFSFVRKMRESRPLMVQTEAQYVF 1082
Cdd:cd14609    233 VLNRM-AKGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

857-1084

1.14e-49

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: 176.56 E-value: 1.14e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  857 AKNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGL-WSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:cd14612     17 SKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYdGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 aGRVKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVRELLLlQVEEQKTlSVRQFHYQAWPDHGVPSSPDTLLAFWRML 1014
Cdd:cd14612     97 -KKEKCVHYWP--EKEGTYGRFEIRVQDMKECDGYTIRDLTI-QLEEESR-SVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1015 RQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:cd14612    172 EESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

885-1091

9.27e-48

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: 169.94 E-value: 9.27e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPC---THGHLRVT 959
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdalTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  960 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW---RMLRQWLDQTMEG---GPPI-VHCS 1032
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLeeiNSVRRHTNQDVAGhnrNPPTlVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1033 AGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFL 1091
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

834-1092

2.76e-47

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: 170.95 E-value: 2.76e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  834 EYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPIHEEPgSDYINASFMPGLWSPQE--FIATQGPLPQTV 911
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  912 GDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVTL-----VGEEVMENWTVRELLLLQveeQK 983
Cdd:cd14599     96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPkLGSKhsSATYGKFKVTTkfrtdSGCYATTGLKVKHLLSGQ---ER 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  984 TlsVRQFHYQAWPDHGVPSSPDTLLAFW-------RMLRQWLDQTMEGGPPIV-HCSAGVGRTGTLIALDVLLRQLQSEG 1055
Cdd:cd14599    173 T--VWHLQYTDWPDHGCPEEVQGFLSYLeeiqsvrRHTNSMLDSTKNCNPPIVvHCSAGVGRTGVVILTELMIGCLEHNE 250

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462566564 1056 LLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 1092
Cdd:cd14599    251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

858-1085

3.51e-47

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: 168.56 E-value: 3.51e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  858 KNRYRNVLPYDWSRVPLKPIH-EEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 935
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGKEKaFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  936 GRvKCEHYWPldSQPCTHGHLRVTLVGEEVMENWTVRELLLLQveEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLR 1015
Cdd:cd14611     82 NE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1016 QWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14611    157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

885-1085

6.82e-47

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: 166.81 E-value: 6.82e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVKCEHYWPlDSQPCTHGHLRVTLVGEE 964
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLL---LQVEEQKTLsVRQFHYQAWPDHG-VPSSPDTLLAFWRMLRQWLDQTMEgGPPIVHCSAGVGRTGT 1040
Cdd:cd14556     79 IDEDVISRIFRLqntTRPQEGYRM-VQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGE-GPIVVHCLNGVGRSGV 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14556    157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

858-1084

2.50e-46

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: 167.35 E-value: 2.50e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  858 KNRYRNVLPYDWSRVPLK-PIHEEPGSDYINASFMPGLWSPQE-FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEA 935
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTsPDQDDPLSSYINANYIRGYGGEEKvYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  936 GRvKCEHYWPLDSqpCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLsvRQFHYQAWPDHGVPSSPDTLLAFWRMLR 1015
Cdd:cd14613    108 NE-KCTEYWPEEQ--VTYEGIEITVKQVIHADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAPPLLQLVQEVE 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1016 QWLDQTMEG-GPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:cd14613    183 EARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

885-1085

3.19e-44

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: 159.09 E-value: 3.19e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGL--WSPQeFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLD-SQPCTHGHLRVTLV 961
Cdd:cd14539      1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  962 GEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR-MLRQWLDQTMEGGPPIVHCSAGVGRTGT 1040
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEeVHSHYLQQRSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462566564 1041 LIALDVLLRQLQSE-GLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14539    160 FCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

885-1087

4.84e-44

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: 158.76 E-value: 4.84e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGlWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWPLDSQPCtHGHLRVTLVG 962
Cdd:cd14546      1 YINASTIYD-HDPRNpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  963 EEVM-ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRTGTL 1041
Cdd:cd14546     79 EHIWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK--SYRGRSCPIVVHCSDGAGRTGTY 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462566564 1042 IALDVLL-RQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCI 1087
Cdd:cd14546    157 ILIDMVLnRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PHA02742

protein tyrosine phosphatase; Provisional

854-1090

6.87e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 155.93 E-value: 6.87e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKPihEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:PHA02742    51 KNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAGRVKCEHYW-PLDSQPCTHGHLRVTLVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWR 1012
Cdd:PHA02742   129 EDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1013 MLRQwLDQTME---------GGPPI-VHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 1082
Cdd:PHA02742   209 AVRE-ADLKADvdikgenivKEPPIlVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                   ....*...
gi 2462566564 1083 LHQCILRF 1090
Cdd:PHA02742   288 CYFIVLIF 295

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

885-1082

5.22e-41

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: 149.92 E-value: 5.22e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFM--PGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGR-VKCEHYWPL-DSQPCTHGHLRVTL 960
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  961 VGEEVMEN-WTVRELLLLQVE-EQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTmegGPPIVHCSAGVGRT 1038
Cdd:cd17658     81 KKLKHSQHsITLRVLEVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSA---GPIVVHCSAGIGRT 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1039 GTLIALDVLLRQLqsegLLGPFS------FVRKMRESRPLMVQTEAQYVF 1082
Cdd:cd17658    158 GAYCTIHNTIRRI----LEGDMSavdlskTVRKFRSQRIGMVQTQDQYIF 203

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

986-1088

3.48e-39

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 140.96 E-value: 3.48e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   986 SVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL-LGPFSFVR 1064
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 2462566564  1065 KMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALL 104

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

986-1088

3.48e-39

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: 140.96 E-value: 3.48e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   986 SVRQFHYQAWPDHGVPSSPDTLLAFWRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGL-LGPFSFVR 1064
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....
gi 2462566564  1065 KMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALL 104

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

854-1096

4.54e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 147.16 E-value: 4.54e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVplkpiheEPGSDYINASFMPGLwSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCM 933
Cdd:COG5599     41 NGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  934 EAG--RVKCEHYWPLDSQPCTHgHLRVTLVGEEV-MENWTVRELLLLQVEE-QKTLSVRQFHYQAWPDHGVPSSpDTLLA 1009
Cdd:COG5599    113 EISkpKVKMPVYFRQDGEYGKY-EVSSELTESIQlRDGIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISA-EALKN 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1010 FWRMLRQWLD-QTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLgPFSF---VRKMRESR-PLMVQTEAQYVFLh 1084
Cdd:COG5599    191 LADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQI-TLSVeeiVIDMRTSRnGGMVQTSEQLDVL- 268

                          250
                   ....*....|..
gi 2462566564 1085 qcILRFLQQSAQ 1096
Cdd:COG5599    269 --VKLAEQQIRP 278

PHA02738

hypothetical protein; Provisional

855-1104

1.08e-35

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 138.52 E-value: 1.08e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  855 NNAKNRYRNVLPYDWSRVPLkPIHEEPGsDYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME 934
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  935 AGRVKCEHYWP-LDSQPCTHGHLRVTLVGEEVMENWtVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFWRM 1013
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHY-VKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1014 LRQWL-----------DQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVF 1082
Cdd:PHA02738   206 VRQCQkelaqeslqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                          250       260
                   ....*....|....*....|..
gi 2462566564 1083 LHQCILRFLQQSAQAPAEKEVP 1104
Cdd:PHA02738   286 CYRAVKRYVNLTVNKVSKKLIP 307

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

885-1085

1.13e-35

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: 134.37 E-value: 1.13e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGrvKCEHYWPLDSQPCTHGHLRVTLVGEE 964
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDhgvPSSP-DTLLAFWRMLRQWLDQTmeGGPPIVHCSAGVGRT 1038
Cdd:cd14550     79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPN---PCSPiHTVFELINTVQEWAQQR--DGPIVVHDRYGGVQA 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462566564 1039 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14550    154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

PHA02747

protein tyrosine phosphatase; Provisional

813-1084

1.02e-33

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 132.43 E-value: 1.02e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  813 AEDFADhvRKNERDSNCGFADEYQQLSLVGHSQSQMVASASENNAKNRYRNVLPYDWSRVPLKPiHEEPGSDYINASFMP 892
Cdd:PHA02747    11 AIDFLK--RRNQLNCFGIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWID 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  893 GLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCME-AGRVKCEHYWPL--DSQPCTHGHLRVTLvgeevmeNW 969
Cdd:PHA02747    88 GFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLneDGNIDMEDFRIETL-------KT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  970 TVRE---LLLLQVEEQKTLSVRQ---FHYQAWPDHGVPSSPDTLLAFWRML---RQ-----WLDQTMEGGPPIVHCSAGV 1035
Cdd:PHA02747   161 SVRAkyiLTLIEITDKILKDSRKishFQCSEWFEDETPSDHPDFIKFIKIIdinRKksgklFNPKDALLCPIVVHCSDGV 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462566564 1036 GRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLH 1084
Cdd:PHA02747   241 GKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289

PHA02746

protein tyrosine phosphatase; Provisional

854-1087

1.14e-33

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 132.85 E-value: 1.14e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  854 ENNAKNRYRNVLPYDWSRVPLKP-------------------IHEEPGSDYINASFMPGLWSPQEFIATQGPLPQTVGDF 914
Cdd:PHA02746    50 ENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  915 WRLVWEQQSHTLVMLTNcMEAGRVKCEHYW--PLDSQpCTHGHLRVTLVgeEVME--NWTVRELLLLQVEEQKTLSVRQF 990
Cdd:PHA02746   130 FKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSE-LAFGRFVAKIL--DIIEelSFTKTRLMITDKISDTSREIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  991 HYQAWPDHGVPSSPDTLLAFW--------RMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALDVLLRQLQSEGLLGPFSF 1062
Cdd:PHA02746   206 WFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 2462566564 1063 VRKMRESRPLMVQTEAQYVFLHQCI 1087
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

885-1088

2.31e-32

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: 125.13 E-value: 2.31e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLtNCMEAGRVkCEHYWPlDSQPCTHGHLRVTLVGEE 964
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKT--LSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTGT 1040
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

885-1092

8.75e-32

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: 123.93 E-value: 8.75e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQE--FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWP-LDSQ--PCTHGHLRVT 959
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrLGSRhnTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  960 LVGEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW-------RMLRQWLDQTMEGGPPIVHCS 1032
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPNPPVLVHCS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1033 AGVGRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQ 1092
Cdd:cd14598    161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

885-1088

9.72e-30

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: 117.40 E-value: 9.72e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEhYWPLDSQPCTHGHLRVTLVGEE 964
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAEE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDhgvPSSP-DTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRT 1038
Cdd:cd17669     80 HKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKE--EAANRDGPMIVHDEHGGVTA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1039 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd17669    155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

885-1088

3.28e-28

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: 113.20 E-value: 3.28e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNC-MEAGrvkCEHYWPLDSQpCTHGHLRVTLVGE 963
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGM-LRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVMENWTVR--ELLLLQVEEQKTLSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTG 1039
Cdd:cd14636     77 SMDCDVISRifRICNLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGeGRTIIHCLNGGGRSG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462566564 1040 TLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

885-1088

1.39e-27

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: 111.32 E-value: 1.39e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRvkCEHYWPlDSQPCTHGHLRVTLVGEE 964
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  965 VMENWTVRELLLLQVEEQKT--LSVRQFHYQAWPDH-GVPSSPDTLLAFWRMLRQWLDQTMEG-GPPIVHCSAGVGRTGT 1040
Cdd:cd14635     78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

885-1088

1.90e-27

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: 110.92 E-value: 1.90e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNcmEAGRVKCEH-YWPLDSQPCTHGHLRVTLVGE 963
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVM-----ENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSpdTLLAFWRMLRQwlDQTMEGGPPIVHCSAGVGRT 1038
Cdd:cd17670     79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS--STFELINVIKE--EALTRDGPTIVHDEFGAVSA 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1039 GTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd17670    155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

885-1088

3.48e-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: 107.30 E-value: 3.48e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  885 YINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRV-KCEHYWPlDSQPCTHGHLRVTLVGE 963
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  964 EVMENWTVRELLLLQVE--EQKTLSVRQFHYQAW-PDHGVPSSPDTLLAFWRMLRQWLDQTMEgGPPIVHCSAGVGRTGT 1040
Cdd:cd14637     80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGE-GRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462566564 1041 LIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCIL 1088
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

900-1083

2.90e-15

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: 76.28 E-value: 2.90e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  900 FIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAGRVKCEHYWpldSQPCTHGhlRVTLVGEEVMENWTVRELL---- 975
Cdd:cd14559     31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF---RQSGTYG--SVTVKSKKTGKDELVDGLKadmy 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  976 LLQV-EEQKTLSVRQFHYQAWPDHGVPSSPDTllafwRMLRQWLDQTMEGGP------------------PIVHCSAGVG 1036
Cdd:cd14559    106 NLKItDGNKTITIPVVHVTNWPDHTAISSEGL-----KELADLVNKSAEEKRnfykskgssaindknkllPVIHCRAGVG 180

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462566564 1037 RTGTLIALDVLLRQLQSEGLLgpfSFVRKMRESR-PLMVQTEAQYVFL 1083
Cdd:cd14559    181 RTGQLAAAMELNKSPNNLSVE---DIVSDMRTSRnGKMVQKDEQLDTL 225

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

958-1085

1.18e-12

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: 66.90 E-value: 1.18e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  958 VTLVGEEVMENWTVRELLllqvEEQKTLSVRQFHYqAWPDHGVPSSpdtlLAFWRMLRQWLDQTMEGGPPIV-HCSAGVG 1036
Cdd:cd14505     48 VTLCTDGELEELGVPDLL----EQYQQAGITWHHL-PIPDGGVPSD----IAQWQELLEELLSALENGKKVLiHCKGGLG 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462566564 1037 RTGTLIAldVLLrqLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:cd14505    119 RTGLIAA--CLL--LELGDTLDPEQAIAAVRALRPGAIQTPKQENFLHQ 163

FN3

Fibronectin type 3 domain [General function prediction only];

261-698

3.32e-12

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 70.80 E-value: 3.32e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  261 TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNS----SVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPD 336
Cdd:COG3401     84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTattaTAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  337 GPDPQNSTYGVEYTGDGGRAGTRSTAHT-NITVDRLEPGCLYVFSVWVGKNGINSSRETR----NATTAPNPVRNLHMET 411
Cdd:COG3401    164 AGAGVVVSPDTSATAAVATTSLTVTSTTlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTTPPSAPTGLTATA 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  412 QTNSSIALCWEVPDGPYPQdyTYWVEYTGDGGGTETR--NTTNTSVTAERLEPGTLYTFSVWAEKNGARGSRQNVSIS-- 487
Cdd:COG3401    244 DTPGSVTLSWDPVTESDAT--GYRVYRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSvt 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  488 ---TVPNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPRTQSTSGTDITLKELEAGSLYHLTVWAER 564
Cdd:COG3401    322 tdlTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVD 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  565 ---------NEVRGYNSTLTAATAPNEVTDLqNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRGQDPQANWVN 635
Cdd:COG3401    402 aagnesapsEEVSATTASAASGESLTASVDA-VPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566564  636 QTSRTNETWYKVEALEPGTLYNFTVWAE-RNDVASSTQSLYPDTVTITSCVSTSAGYGVNLIWS 698
Cdd:COG3401    481 TTDTTTANLSVTTGSLVGGSGASSVTNSvSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544

PHA02740

protein tyrosine phosphatase; Provisional

807-1094

1.60e-11

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 66.53 E-value: 1.60e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  807 SPGDIPAEDFADHVRKNerDSNCGFADEYQQLsLVGHSQSQMVASASENNAKNRYRNVLP---YDWSRVPLKPiheepGS 883
Cdd:PHA02740     5 DAVDINGMDFINFINKP--DLLSCIIKEYRAI-VPEHEDEANKACAQAENKAKDENLALHitrLLHRRIKLFN-----DE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  884 DYINASFMPGLWSPQEFIATQGPLPQTVGDFWRLVWEQQSHTLVMLTNCMEAgrvKC-EHYWPLDSQPC-THGHLRVTLV 961
Cdd:PHA02740    77 KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  962 gEEVMENWTVRELLLLQVEEQKTLSVRQFHYQAWPDHGVPSSPDTLLAFW----RMLRQWLDQTMEG--GPPIVHCSAGV 1035
Cdd:PHA02740   154 -EIIIKPHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFcnidDLCADLEKHKADGkiAPIIIDCIDGI 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564 1036 GRTGTLIALDVLLRQLQSEGLLGPFSFVRKMRESRPLMVQTEAQYVFLHQCILRFLQQS 1094
Cdd:PHA02740   233 SSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

962-1085

6.28e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 61.53 E-value: 6.28e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  962 GEEVMENWTVRELLLLQVEEQKTLSVR-----QFHYQAWPDHGVPSSPDtllafWRMLRQWLDQTMEGGPPI-VHCSAGV 1035
Cdd:COG2453     17 GEADLKREGIDAVVSLTEEEELLLGLLeeaglEYLHLPIPDFGAPDDEQ-----LQEAVDFIDEALREGKKVlVHCRGGI 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462566564 1036 GRTGTLIALdVLLRQlqseGLlgpfSF---VRKMRESRPLMVQTEAQYVFLHQ 1085
Cdd:COG2453     92 GRTGTVAAA-YLVLL----GL----SAeeaLARVRAARPGAVETPAQRAFLER 135

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

401-479

8.53e-11

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 59.43 E-value: 8.53e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  401 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGT----ETRNTTNTSVTAERLEPGTLYTFSVWAEKNG 476
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ...
gi 2462566564  477 ARG 479
Cdd:cd00063     81 GES 83

FN3

Fibronectin type 3 domain [General function prediction only];

51-529

1.98e-10

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 65.02 E-value: 1.98e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   51 LTVETQTTSSISLSWEVPDGLDSQNSNYWV-QCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVWVEKDGVNSSVGTVT 129
Cdd:COG3401     55 LLVAAGLSSGGGLGTGGRAGTTSGVAAVAVaAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGG 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  130 TATAPNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGGRAGTRSTAHT-NITVDGLEPGCLYAFSMWVGKN 208
Cdd:COG3401    135 AATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTlVDGGGDIEPGTTYYYRVAATDT 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  209 GINSSRETR----NATTAHNPVRNLRVEAQTTSSISLSWEvpDGTDPQNSTYCV--QCTGDGGRTETRNTTDTRVTVDGL 282
Cdd:COG3401    215 GGESAPSNEvsvtTPTTPPSAPTGLTATADTPGSVTLSWD--PVTESDATGYRVyrSNSGDGPFTKVATVTTTSYTDTGL 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  283 GPGSLYTCSVW-VEKDGVNS----SVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPqnSTYGVEYTGDGGRAG 357
Cdd:COG3401    293 TNGTTYYYRVTaVDAAGNESapsnVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVYRSTSGGGTY 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  358 T---RSTAHTNITVDRLEPGCLYVFSV-----------------------WVGKNGINSSRETRNATTAPNPVRNLHMET 411
Cdd:COG3401    371 TkiaETVTTTSYTDTGLTPGTTYYYKVtavdaagnesapseevsattasaASGESLTASVDAVPLTDVAGATAAASAASN 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  412 QTNSSIalcWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTNTSVTAERLEPGTLYTFSVWAEKN-GARGSRQNVSISTVP 490
Cdd:COG3401    451 PGVSAA---VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSViGASAAAAVGGAPDGT 527

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2462566564  491 NAVTSLSKQDWTNSTiALRWTAPQGPGQSSYSYWVSWVR 529
Cdd:COG3401    528 PNVTGASPVTVGAST-GDVLITDLVSLTTSASSSVSGAG 565

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

1008-1085

3.07e-10

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: 58.52 E-value: 3.07e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564 1008 LAFWRMLRQWLDQTMEGGPPI-VHCSAGVGRTGTLIALDVLLRQLQSegllgPFSFVRKMRESRP-LMVQTEAQYVFLHQ 1085
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRPgGIPQTIEQLDFLIK 113

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

401-473

5.82e-10

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.85 E-value: 5.82e-10

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462566564   401 PNPVRNLHMETQTNSSIALCWEVPDGPYPQDYT--YWVEYTGDGGGTETRNTTN--TSVTAERLEPGTLYTFSVWAE 473
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

580-663

1.09e-09

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 56.08 E-value: 1.09e-09

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   580 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYV--YWVQWaskghprrgQDPQANWVNQTSRTNETWYKVEALEPGTLYN 657
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgYRVEY---------REEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71


                    ....*.
gi 2462566564   658 FTVWAE 663
Cdd:smart00060   72 FRVRAV 77

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

312-399

3.02e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 55.20 E-value: 3.02e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  312 PNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDRLEPGCLYVFSVW-VGKN 386
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                           90
                   ....*....|...
gi 2462566564  387 GINSSRETRNATT 399
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

224-307

5.02e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 54.42 E-value: 5.02e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  224 NPVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQCTGDGGRT----ETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGV 299
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 2462566564  300 NS----SVEIVT 307
Cdd:cd00063     82 ESppseSVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

580-669

7.00e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 54.04 E-value: 7.00e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  580 PNEVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRrgqdpqanWVN-QTSRTNETWYKVEALEPGTLYNF 658
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD--------WKEvEVTPGSETSYTLTGLKPGTEYEF 72

                           90
                   ....*....|.
gi 2462566564  659 TVWAERNDVAS 669
Cdd:cd00063     73 RVRAVNGGGES 83

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

134-221

9.84e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.65 E-value: 9.84e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  134 PNPVRNLRVEAQTNSSIALTWEVPDGPDPQNSTYGVEYTGDGG----RAGTRSTAHTNITVDGLEPGCLYAFSMW-VGKN 208
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSgdwkEVEVTPGSETSYTLTGLKPGTEYEFRVRaVNGG 80

                           90
                   ....*....|...
gi 2462566564  209 GINSSRETRNATT 221
Cdd:cd00063     81 GESPPSESVTVTT 93

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

45-132

1.20e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 53.27 E-value: 1.20e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   45 PNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTT----ETRNTTATNVTVDGLGPGSLYTCSVWVEKDG 120
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 2462566564  121 VNSSVGTVTTAT 132
Cdd:cd00063     81 GESPPSESVTVT 92

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

990-1084

7.75e-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: 7.75e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  990 FHYQAWPDHGVPSsPDTLLAFWRMLRQWLDqtmEGGPPIVHCSAGVGRTGTLIA--LDVLLRqlqseglLGPFSFVRKMR 1067
Cdd:cd14506     79 FYNFGWKDYGVPS-LTTILDIVKVMAFALQ---EGGKVAVHCHAGLGRTGVLIAcyLVYALR-------MSADQAIRLVR 147

                           90
                   ....*....|....*..
gi 2462566564 1068 ESRPLMVQTEAQYVFLH 1084
Cdd:cd14506    148 SKRPNSIQTRGQVLCVR 164

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

312-383

2.21e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 49.54 E-value: 2.21e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566564   312 PNPVRNLTVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDRLEPGCLYVFSVWV 383
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76

FN3

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

490-578

3.74e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 3.74e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  490 PNAVTSLSKQDWTNSTIALRWTAPQGPGQSSYSYWVSWVREGMTDPR---TQSTSGTDITLKELEAGSLYHLTVWAERNE 566
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKeveVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 2462566564  567 VRGYNSTLTAAT 578
Cdd:cd00063     81 GESPPSESVTVT 92

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

225-301

6.11e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.38 E-value: 6.11e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   225 PVRNLRVEAQTTSSISLSWEVP--DGTDPQNSTYCVQCTGDGGRTETRNTT--DTRVTVDGLGPGSLYTCSVWVEKDGVN 300
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTpsSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 2462566564   301 S 301
Cdd:smart00060   83 G 83

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

134-205

8.36e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 47.99 E-value: 8.36e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566564   134 PNPVRNLRVEAQTNSSIALTWEVPdgPDPQNSTYGVEYTGDGGRAG------TRSTAHTNITVDGLEPGCLYAFSMWV 205
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPP--PDDGITGYIVGYRVEYREEGsewkevNVTPSSTSYTLTGLKPGTEYEFRVRA 76

fn3

Fibronectin type III domain;

582-660

2.85e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.25 E-value: 2.85e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566564  582 EVTDLQNETQTKNSVMLWWKAPGDPHSQLYVYWVQWASKGHPRRgqdpqanWVNQTSRTNETWYKVEALEPGTLYNFTV 660
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEP-------WNEITVPGTTTSVTLTGLKPGTEYEVRV 73

fn3

Fibronectin type III domain;

225-292

4.98e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 4.98e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462566564  225 PVRNLRVEAQTTSSISLSWEVPDGTDPQNSTYCVQC----TGDGGRTETRNTTDTRVTVDGLGPGSLYTCSV 292
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

Fibronectin type 3 domain [General function prediction only];

44-368

6.44e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.39 E-value: 6.44e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564   44 APNPGRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATNVTVDGLGPGSLYTCSVW-VEKDGV- 121
Cdd:COG3401    232 PPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTaVDAAGNe 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  122 --NSSVGTVTTA-TAPNPVRNLRVEAQTNSSIALTWEVPDGPDPqnSTYGVEYTGDGGRAGT---RSTAHTNITVDGLEP 195
Cdd:COG3401    312 saPSNVVSVTTDlTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVYRSTSGGGTYTkiaETVTTTSYTDTGLTP 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  196 GCLYAFS-MWVGKNGINSSR---------ETRNATTAHNPVRNLRVEAQTTSSISLSWEVPDGTDPQNstycvqcTGDGG 265
Cdd:COG3401    390 GTTYYYKvTAVDAAGNESAPseevsattaSAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAV-------LADGG 462

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  266 RTETRNTTDTRVTVDGLGPGSLYTCSVWVEKDGVNSSVEIVTSATAPNPVRNLTVEAQTNSSIALTWEVPDGPDPQNSTY 345
Cdd:COG3401    463 DTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAST 542

                          330       340
                   ....*....|....*....|...
gi 2462566564  346 GVEYTGDGGRAGTRSTAHTNITV 368
Cdd:COG3401    543 GDVLITDLVSLTTSASSSVSGAG 565

fn3

Fibronectin type III domain;

403-479

1.07e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 44.71 E-value: 1.07e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  403 PVRNLHMETQTNSSIALCWEVPDGPYPQDYTYWVEYTGDGGGTETRNTTN----TSVTAERLEPGTLYTFSVWAEKNGAR 478
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVpgttTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   .
gi 2462566564  479 G 479
Cdd:pfam00041   82 G 82

FN3

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

45-123

1.75e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.14 E-value: 1.75e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564    45 PNPGRNLTVETQTTSSISLSWEVP--DGLDSQNSNYWVQCTGDGGTTE--TRNTTATNVTVDGLGPGSLYTCSVWVEKDG 120
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKevNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 2462566564   121 VNS 123
Cdd:smart00060   81 GEG 83

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

996-1085

3.43e-05

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

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 44.96 E-value: 3.43e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  996 PDHGVPSSPDTLlafwRMLRQWLDQTMEGGPPIVHCSAGVGRTGTLIALdvllrQLQSEGLLGPFSFVRKMRESRPLMVQ 1075
Cdd:cd14504     58 EDYTPPTLEQID----EFLDIVEEANAKNEAVLVHCLAGKGRTGTMLAC-----YLVKTGKISAVDAINEIRRIRPGSIE 128

                           90
                   ....*....|
gi 2462566564 1076 TEAQYVFLHQ 1085
Cdd:cd14504    129 TSEQEKFVIQ 138

CDC14_C

cd14499

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...

996-1044

6.92e-05

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 44.75 E-value: 6.92e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462566564  996 PDHGVPSspdtllafWRMLRQWLDQT-MEGGPPIVHCSAGVGRTGTLIAL 1044
Cdd:cd14499     88 PDGSTPS--------DDIVKKFLDICeNEKGAIAVHCKAGLGRTGTLIAC 129

fn3

Fibronectin type III domain;

43-114

7.70e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.40 E-value: 7.70e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566564   43 PAPnpgRNLTVETQTTSSISLSWEVPDGLDSQNSNYWVQCTGDGGTTETRNTTATN----VTVDGLGPGSLYTCSV 114
Cdd:pfam00041    1 SAP---SNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtttsVTLTGLKPGTEYEVRV 73

fn3

Fibronectin type III domain;

314-394

7.77e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.40 E-value: 7.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566564  314 PVRNLTVEAQTNSSIALTWEVPDGPDPQNSTYGVEY----TGDGGRAGTRSTAHTNITVDRLEPGCLYVFSVwVGKNGIN 389
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYrpknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV-QAVNGGG 80


                   ....*
gi 2462566564  390 SSRET 394
Cdd:pfam00041   81 EGPPS 85

fn3